Crystal structure

ABSTRACT

The invention provides a method of predicting a three dimensional structural representation of a target protein of unknown structure, or part thereof, comprising: providing the coordinates of the turkey β1-AR structure listed in Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 A, or selected coordinates thereof; and predicting the three-dimensional structural representation of the target protein, or part thereof, by modelling the structural representation on all or the selected coordinates of the turkey β1-AR. The invention also provides the use of the turkey β1-AR coordinates to select or design one or more binding partners of β1-AR.

The present invention relates to protein crystal structures and their use in identifying protein binding partners and in protein structure determination. In particular, it relates to the crystal structure of a ββ-adrenergic receptor (β1-AR) and uses thereof.

The listing or discussion of an apparently prior-published document in this specification should not necessarily be taken as an acknowledgement that the document is part of the state of the art or is common general knowledge.

G protein-coupled receptors (GPCRs) are a large family of integral membrane proteins that are ubiquitous in eukaryotes from yeast to man, which function as key intermediaries in the transduction of signals from the outside of the cell to the inside. Activating molecules (agonists), such as hormones and neurotransmitters, bind to the GPCRs at the cell surface and cause a conformational change at the cytoplasmic surface, resulting in the activation of G proteins and the resultant increase in intracellular messengers such as cAMP, Ca²⁺ and signalling lipids. The central role of GPCRs in signalling throughout the body makes them ideal targets for therapeutic agents and, in fact, about 30% of prescription drugs mediate their effects by binding specifically to GPCRs and it is thought that developing new specific compounds to inhibit or activate other GPCRs could represent a major route to the development of new drugs.

There are about 850 different GPCRs in the human body and they all share the characteristic of 7 transmembrane domains with their N terminus in the extracellular side of the plasma membrane. Analysis of their primary amino acid sequence has resulted in the definition of a number of subfamilies, the largest of which, Family A, includes the archetypal GPCR, rhodopsin. One of the subdivisions within Family A contains the aminergic receptors, which include, for example, serotonin, dopamine, acetylcholine and adrenergic receptors. The natural ligand for adrenergic receptors is either adrenaline, released into the blood from the adrenal glands, or noradrenaline, which is a neurotransmitter in the brain, but also acts peripherally. The adrenergic receptors are further divided into two groups, the α- and β-adrenergic receptors, originally classified depending on whether they caused contraction or relaxation of tissues. There are three β-adrenergic (β-AR) subtypes in humans, β1, β2 and β3 and they share 53% sequence identity, excluding the N- and C-termini and inner loop 3. There is a wealth of pharmacology associated with the βARs, because molecules that inhibit receptor signalling (antagonists) are capable of modulating the function of the heart and are commonly known as β-blockers. Non-selective β-blockers such as propranolol were used in treatment of hypertension or for cardioprotection after a heart attack (inhibition of the β1-AR), but more recently selective β1-antagonists are preferred since they have fewer side effects due to bronchial constriction (β2 effect). The development of β-blockers followed classical pharmacological characterisation of small molecules that inhibited signalling of βARs, which has resulted in a multitude of compounds that differentially effect the three different subtypes (Baker J G (2005) British Journal Pharmanol. Vol 144, pp 317-322). However, it has been unclear what determines the specificity of drug binding to the specific subtypes; elucidation of this mechanism will allow the development of more subtype-specific β-blockers and hence reduce side-effects for various patient groups.

Two independently determined structures of the β2-adrenergic receptor (β2-AR) that both contained bound antagonist (specifically, a partial inverse agonist) carazolol have recently been published (Rasmussen et al 2007; Cherezov et al 2007). The structures define the overall architecture of the protein and provide a description of the ligand binding region and how amino acid residues contribute to the specificity of the ligand bound. However, the structures also raise many questions of how different βARs bind the same ligand with different affinities. For example, the human β1 and β2 receptors are 69% identical within their transmembrane regions, but if only the residues that were predicted to surround the ligand binding region in the β2 structure are considered, then the receptors are apparently identical. Despite these similarities, compounds such as CGP20712A bind 500 times more strongly to the β1 receptor than to the β2 receptor, whilst ICI 118551 shows a 550 fold specificity for the β2 receptor over β1 (Baker J G (2005) British Journal Pharmacol. Vol 144, pp 317-322). Ideally, the structures of both the β1 and β2 receptors need to be compared to elucidate the mechanism behind drug discrimination.

We have now crystallised and determined the first structure of a β1-AR, the turkey β1-AR, in complex with the antagonist cyanopindolol using X-ray crystallography. Crystals of a stabilised mutant turkey β1-AR receptor (β1-AR-m23) were crystallised in a variety of detergents and conditions, giving rise to two predominant forms with either C2 or P1 geometry. In both space groups there were four molecules per unit cell (molecules A-D). The structure was solved to a resolution of 2.7 Å by molecular replacement using the coordinates of the β2-AR (Cherezov et al, 2007). The atomic coordinates of molecules A-D are provided in Tables A-D respectively.

The coordinates of the β1-AR can be utilised and manipulated in many different ways with wide ranging applications including the fitting of binding partners, homology modelling and structure solution, analysis of ligand interactions and drug discovery.

Accordingly, a first aspect of the invention provides a method of predicting a three dimensional structural representation of a target protein of unknown structure, or part thereof, comprising:

-   -   providing the coordinates of the turkey β1-AR structure listed         in Table A, Table B, Table C or Table D, optionally varied by a         root mean square deviation of residue backbone atoms of not more         than 1.235 Å, or selected coordinates thereof; and     -   predicting the three-dimensional structural representation of         the target protein, or part thereof, by modelling the structural         representation on all or the selected coordinates of the turkey         β1-AR.

By a ‘three dimensional structural representation’ we include a computer generated representation or a physical representation. Typically, in all aspects of the invention which feature a structural representation, the representation is computer generated. Computer representations can be generated or displayed by commercially available software programs. Examples of software programs include but are not limited to QUANTA (Accelrys. COPYRIGHT. 2001, 2002), O (Jones et al., Acta Crystallogr. A47, pp. 110-119 (1991)) and RIBBONS (Carson, J. Appl. Crystallogr., 24, pp. 9589-961 (1991)), which are incorporated herein by reference. Examples of representations include any of a wire-frame model, a chicken-wire model, a ball-and-stick model, a space-filling model, a stick model, a ribbon model, a snake model, an arrow and cylinder model, an electron density map or a molecular surface model. Certain software programs may also imbue these three dimensional representations with physico-chemical attributes which are known from the chemical composition of the molecule, such as residue charge, hydrophobicity, torsional and rotational degrees of freedom for the residue or segment, etc. Examples of software programs for calculating chemical energies are described below.

Typically, the coordinates of the turkey β1-AR structure used in the invention are those listed in Table A, Table B, Table C or Table D. Preferably the coordinates used are of molecule B in Table B. However, it is appreciated that it is not necessary to have recourse to the original coordinates listed in Table A, Table B, Table C or Table D and that any equivalent geometric representation derived from or obtained by reference to the original coordinates may be used.

Thus, for the avoidance of doubt, by ‘the coordinates of the turkey β1-AR structure listed in Table A, Table B, Table C or Table D’, we include any equivalent representation wherein the original coordinates have been reparameterised in some way. For example, the coordinates in Table A, Table B, Table C or Table D may undergo any mathematical transformation known in the art, such as a geometric transformation, and the resulting transformed coordinates can be used. For example, the coordinates of Table A, Table B, Table C or Table D may be transposed to a different origin and/or axes or may be rotated about an axis. Furthermore, it is possible to use the coordinates to calculate the psi and phi backbone torsion angles (as displayed on a Ramachandran plot) and the chi sidechain torsion angles for each residue in the protein. These angles together with the corresponding bond lengths, enable the construction of a geometric representation of the protein which may be used based on the parameters of psi, phi and chi angles and bond lengths. Thus while the coordinates used are typically those in Table A, Table B, Table C or Table D, the inventors recognise that any equivalent geometric representation of the turkey β1-AR structure, based on the coordinates listed in Table A, Table B, Table C or Table D, may be used.

Additionally, it is appreciated that changing the number and/or positions of the water molecules and/or ligand molecule of the Tables does not generally affect the usefulness of the coordinates in the aspects of the invention. Thus, it is also within the scope of the invention if the number and/or positions of water molecules and/or ligand molecules of the coordinates of Table A, Table B, Table C or Table D is varied.

It will be appreciated that in all aspects of the invention which utilise the coordinates of the turkey β1-AR, it is not necessary to utilise all the coordinates of Table A, Table B, Table C or Table D, but merely a portion of them, e.g. a set of coordinates representing atoms of particular interest in relation to a particular use. Such a portion of coordinates is referred to herein as ‘selected coordinates’.

By ‘selected coordinates’, we include at least 5, 10 or 20 non-hydrogen protein atoms of the turkey β1-AR structure, more preferably at least 50, 100, 200, 300, 400, 500, 600, 700, 800 or 900 atoms and even more preferably at least 1000, 1100, 1200, 1300, 1400, 1500, 1600, 1700, 1800, 1900, 2000, 2100 or 2200 non-hydrogen atoms. Preferably the selected coordinates pertain to at least 0.5, 10, 20 or 30 different amino acid residues (i.e. at least one atom from 5, 10, 20 or 30 different residues may be present), more preferably at least 40, 50, 60, 70, 80 or 90 residues, and even more preferably at least 100, 150, 200, 250 or 300 residues. Optionally, the selected coordinates may include one or more ligand atoms and/or water atoms and/or sodium atoms as set out in Table A, Table B, Table C or Table D. Alternatively, the selected coordinates may exclude one or more water atoms or sodium atoms or may exclude one or more atoms of the ligand.

In one example, the selected coordinates may comprise atoms of one or more amino acid residues that contribute to the main chain or side chain atoms of a binding region of the turkey β1-AR. For example, amino acid residues contributing to the ligand binding site include amino acid residues 117, 118, 121, 122, 125, 201, 203, 207, 211, 215, 306, 307, 310 and 329, according to the numbering of turkey β1-AR as set out in FIG. 6, all of which make direct contact to the ligand cyanopindolol ligand. Thus the selected coordinates may comprise one or more atoms from any one or more of amino acid residues 117, 118, 121, 122, 125, 201, 203, 207, 211, 215, 306, 307, 310 and 329, according to the numbering of turkey β1-AR as set out in FIG. 6. Typically, coordinates of all of the atoms of the side chain are selected.

In another example, the selected coordinates may comprise atoms which coordinate a sodium ion. For example, an interesting observation of the β1-AR structure is the presence of a well coordinated sodium ion at the C-terminus of the short extracellular loop-1 (EL1) helix in a location often found for positive ions or ligands at the negative end of the α-helix dipole. The sodium ion is coordinated by the carbonyl groups in the peptide backbone from residues Cys 192, Asp 195 and Cys 198 and one water molecule. Thus, the selected coordinates may comprise one or more (for example all atoms of the side chain) atoms of any one or more of these residues and the water molecule which coordinates the sodium ion.

In a further example, the selected coordinates may comprise atoms of one or more amino acids in cytoplasmic loop-2 (CL2) which mediates coupling of the GPCR to G proteins when in the activated state. The cytoplasmic loop structure of CL2 in β1-AR is significantly different from that in β2-AR despite the amino acid sequence of CL2 being almost identical in the β-AR family. Specifically, CL2 in β1-AR is a well-structured short α-helix, whereas in the β2 structures CL2 is unstructured. Thus, the selected coordinates may comprise atoms of one or more of amino acid residues Ser 145, Pro 146, Phe 147, Arg 148, Tyr 149, Gln 150, Ser 151, Leu 152, Met 153 and Thr 154.

In another example, the selected coordinates may comprise atoms of one or more amino acids which define the conserved DRY motif in helix 3 of GPCRs. The DRY motif has been implicated both in G protein coupling and in the regulation of receptor activation (Rovati et al 2007, Mol Pharmacol 71(4): 959). Thus, the selected coordinates may comprise atoms of one or more of amino acid residues Asp 138, Arg 139 and Tyr 140.

In a further example, the selected coordinates may comprise atoms of one or more of the amino acids that define the binding region and are highly conserved in β1-ARs but not in β2-ARs. For example, residues Val 172 and Phe 325 are highly conserved in the β1 receptor but not in the β2 receptor whereas equivalent residues Thr 164 and Tyr 308 are highly conserved in the β2 receptor but not in the β1 receptor. Therefore, these residues are believed to have a profound effect upon ligand binding and selectivity. Thus, the selected coordinates may comprise atoms of Val 172 and/or Phe 325.

In yet a further example, the selected coordinates may comprise atoms of one or more of the amino acids in β1-AR which have been shown to be important in β1 versus β2 selectivity for particular ligands. For example amino residues Leu 110, Thr 117 and Phe 359 in β1-AR have been demonstrated to be important for the β1 selectivity of ligand RO363 (Sugimoto et al, 2002). Thus, the selected coordinates may comprise atoms of one or more of amino acids Leu 110, Thr 117 and Phe 359.

In another example, the selected coordinates may comprise atoms of an amino acid residue, mutation of which is a known polymorphism in the human β1AR family. For example, the human β1-AR mutation R389G corresponds to turkey β1-AR Arg 355 in C-terminal helix 8 and has a marked effect on in vitro function. Thus, the selected coordinates may comprise atoms of amino acid Arg 355.

It is appreciated that the selected coordinates may comprise any atoms of particular interest including atoms mentioned in any one or more of the above examples.

Preferably, the selected coordinates include at least 2% or 5% C-α atoms, and more preferably at least 10% C-α atoms. Alternatively or additionally, the selected coordinates include at least 10% and more preferably at least 20% or 30% backbone atoms selected from any combination of the nitrogen, C-α, carbonyl C and carbonyl oxygen atoms.

It is appreciated that the coordinates of the turkey β1-AR used in the invention may be optionally varied and a subset of the coordinates or the varied coordinates may be selected (and constitute selected coordinates). Indeed, such variation may be necessary in various aspects of the invention, for example in the modelling of protein structures and in the fitting of various binding partners to the β1-AR structure.

Protein structure variability and similarity is routinely expressed and measured by the root mean square deviation (rmsd), which measures the difference in positioning in space between two sets of atoms. The rmsd measures distance between equivalent atoms after their optimal superposition. The rmsd can be calculated over all atoms, over residue backbone atoms (i.e. the nitrogen-carbon-carbon backbone atoms of the protein amino acid residues), main chain atoms only (i.e. the nitrogen-carbon-oxygen-carbon backbone atoms of the protein amino acid residues), side chain atoms only or more usually over C-α atoms only.

The least-squares algorithms used to calculate rmsd are well known in the art and include those described by Rossman and Argos (J Biol Chem, (1975) 250:7525), Kabsch (Acta Cryst (1976) A92:922; Acta Cryst (1978) A34:827-828), Hendrickson (Acta Cryst (1979) A35: 158), McLachan (J Mol Biol (1979) 128:49) and Kearsley (Acta Cryst (1989) A45:208). Both algorithms based on iteration in which one molecule is moved relative to the other, such as that described by Ferro and Hermans (Acta Cryst (1977) A33:345-347), and algorithms which locate the best fit directly (e.g. Kabsch's methods) may be used. Methods of comparing proteins structures are also discussed in Methods of Enzymology, vol 115: 397-420.

Typically, rmsd values are calculated using coordinate fitting computer programs and any suitable computer program known in the art may be used, for example MNYFIT (part of a collection of programs called COMPOSER, Sutcliffe et al (1987) Protein Eng 1:377-384). Other programs also include LSQMAN (Kleywegt & Jones (1994) A super position, CCP4/ESF-EACBM, Newsletter on Protein Crystallography, 31: 9-14), LSQKAB (Collaborative Computational Project 4. The CCP4 Suite: Programs for Protein Crystallography, Acta Cryst (1994) D50:760-763), QUANTA (Jones et al, Acta Cryst (1991) A47:110-119 and commercially available from Accelrys, San Diego, Calif.), Insight (Commercially available from Accelrys, San Diego, Calif.), Sybyl® (commercially available from Tripos, Inc., St Louis) and O (Jones et al., Acta Cryst (1991) A47:110-119).

In, for example, the programs LSQKAB and O, the user can define the residues in the two proteins that are to be paired for the purpose of the calculation. Alternatively, the pairing of residues can be determined by generating a sequence alignment of the two proteins as is well known in the art. The atomic coordinates can then be superimposed according to this alignment and an rmsd value calculated. The program Sequoia (Bruns et al (1999) J Mol Biol 288(3):427-439) performs the alignment of homologous protein sequences, and the superposition of homologous protein atomic coordinates. Once aligned, the rmsd can be calculated using programs detailed above. When the sequences are identical or highly similar, the structural alignment of proteins can be done manually or automatically as outlined above. Another approach would be to generate a superposition of protein atomic coordinates without considering the sequence.

We have conducted an rmsd analysis of residue backbone atoms (i.e. the nitrogen-carbon-carbon backbone atoms of the protein) between the β1-AR (molecule B) and the β2-AR (Cherezov et al., 2007) using a LSQMAN script as shown in part B of Example 3. Similar scripts can be used to calculate rmsd values for any other selected coordinates. Rmsd values have been calculated on residue backbone atoms in the complete structure (1.235 Å), on residue backbone atoms used in aligning helices 2-6, on residue backbone atoms within the individual helices and on residue backbone atoms within the individual loop regions. Thus in an embodiment, where the coordinates or selected coordinates used in the invention are optionally varied within a particular structural region of the turkey β1-AR (e.g. helix 3 or just within the helices), they are optionally varied within an rmsd of residue backbone atoms of not more than the value corresponding to that structural region provided in part B of Example 3. For example, if the coordinates or selected coordinates are optionally varied within helix 3, they are optionally varied within an rmsd of residue backbone atoms of not more than 0.304 Å (such as not more than 0.3 Å or 0.2 Å or 0.1 Å) and if the coordinates or selected coordinates are optionally varied within extracellular loop 2, they are optionally varied within an rmsd of residue backbone atoms of not more than 0.836 Å (such as not more than 0.8 Å or 0.7 Å or 0.6 Å or 0.5 Å or 0.4 Å or 0.3 Å or 0.2 Å or 0.1 Å). By the helices and loop regions of the turkey β1-AR we mean the following:

Helix 1 Residues 47-67 Helix 2 Residues 77-98 Helix 3 Residues 117-142 Helix 4 Residues 156-173 Helix 5 Residues 208-237 Helix 6 Residues 286-310 Helix 7 Residues 320-340 Helix 8 Residues 341-358 CL1 Residues 68-76 EL1 Residues 99-116 CL2 Residues 143-155 EL2 Residues 174-207 EL3 Residues 311-319

However, it will be appreciated that there are different criteria for which residues are considered to be in a helical conformation depending on phi and psi angles. Moreover, when comparing the turkey β1-AR to other structures, some residues may be missing in one or other of the structures and some residues may be considered helical in one structure but not the other. Therefore the limits above are not to be construed as absolute, but rather may vary according to the criteria used. Nevertheless, for the purposes of the comparisons set out below, we have used the above-mentioned definitions of helices and loops.

Thus in one embodiment, the coordinates or selected coordinates of Table A, Table B, Table C or Table D may be optionally varied within an rmsd of residue backbone atoms (i.e. the nitrogen-carbon-carbon backbone atoms of the protein) of not more than 1.235 Å. Preferably, the coordinates or selected coordinates are varied within an rmsd of residue backbone atoms of not more than 1.2 Å, 1.1 Å, 1.0 Å, 0.9 Å or 0.8 Å and more preferably not more than 0.7 Å, 0.6 Å, 0.5 Å, 0.4 Å, 0.3 Å, 0.2 Å or 0.1 Å.

Conducting an rmsd analysis of residue backbone atoms between β1-AR (molecule A; where N-terminal 50 residues of Helix 1 are omitted) and β2-AR (Cherezov et al, 2007) gave an rmsd value of 1.25 Å. Thus in one embodiment, the coordinates or selected coordinates of Table A, Table B, Table C or Table D may be optionally varied within an rmsd of residue backbone atoms of not more than 1.25 Å. Preferably, the coordinates or selected coordinates are varied within an rmsd of residue backbone atoms of not more than 1.2 Å, 1.1 Å, 1.0 Å, 0.9 Å or 0.8 Å and more preferably not more than 0.7 Å, 0.6 Å, 0.5 Å, 0.4 Å, 0.3 Å, 0.2 Å or 0.1 Å.

It is appreciated that rmsd can also be calculated over C-α atoms and side chain atoms.

For example, we aligned β1-AR (molecule B) with β2-AR (Cherezov et al, 2007) over the residues in helices 2-6, and a rmsd analysis of residue C-α atoms gave a value of 0.399 Å. The same analysis using β1-AR (molecule A) in the alignment gave a value of 0.401 Å. Thus, in one embodiment, the coordinates or selected coordinates are optionally varied within an rmsd of residue C-α atoms in helices 2-6 of not more than 0.40 Å. Preferably, the coordinates or selected coordinates are varied within an rmsd of residue C-α atoms in helices 2-6 of not more than 0.35 Å, 0.30 Å or 0.25 Å and more preferably not more than 0.2 Å, 0.15 Å or 0.10 Å.

We have conducted an rmsd analysis of residue C-α atoms and residue side chain atoms between β1-AR (molecule B) and β2-AR (Cherezov et al, 2007) within the active site (i.e. residues 117, 118, 121, 122, 125, 201, 203, 207, 211, 215, 306, 307, 310 and 329) as shown in Example 3. The rmsd value for residue C-α atoms is 0.38 Å and for side chain atoms is 0.59 Å. Thus in an embodiment, where the coordinates or selected coordinates used in the invention are optionally varied within the active site, they are varied within an rmsd of C-α atoms of not more than 0.38 Å (such as not more than 0.3 Å or 0.2 Å or 0.1 Å) and/or within an rmsd of side chain atoms of not more than 0.59 Å (such as not more than 0.5 Å or 0.4 Å or 0.3 Å or 0.2 Å or 0.1 Å).

We have conducted an rmsd analysis of residue C-α atoms and residue side chain atoms between β1-AR (molecule B) and β2-AR (Cherezov et al, 2007) within the Na ion coordination site (i.e. residues Cys 192, Asp 195 and Cys 198). The rmsd value for residue C-α atoms is 1.03 Å and for side chain atoms is 1.09 Å. Thus in an embodiment, where the coordinates or selected coordinates used in the invention are optionally varied within the Na ion coordination site, they are varied within an rmsd of C-α atoms of not more than 1.03 Å (such as not more than 1 Å or 0.9 Å or 0.8 Å or 0.7 Å or 0.6 Å or 0.5 Å or 0.4 Å or 0.3 Å or 0.2 Å or 0.1 Å) and/or within an rmsd of side chain atoms of not more than 1.09 Å (such as not more than 1 Å or 0.9 Å or 0.8 Å or 0.7 Å or 0.6 Å or 0.5 Å or 0.4 Å or 0.3 Å or 0.2 Å or 0.1 Å).

We have conducted an rmsd analysis of residue C-α atoms and residue side chain atoms between β1-AR (molecule B) and 62-AR (Cherezov et al, 2007) within the CL2 (i.e. residues 145-154). The rmsd value for residue C-α atoms is 5.66 Å and for side chain atoms is 6.88 Å. Thus in an embodiment, where the coordinates or selected coordinates used in the invention are optionally varied within the CL2, they are varied within an rmsd of C-α atoms of not more than 5.66 Å (such as not more than 5.5 Å or 5 Å or 4.5 Å or 4 Å or 3.5 Å or 3 Å or 2.5 Å or 2 Å or 1.5 Å or 1 Å or 0.5 Å) and/or within an rmsd of side chain atoms of not more than 6.88 Å (such as not more than 6.5 Å or 6 Å or 5.5 Å or 5 Å or 4.5 Å or 4 Å or 3.5 Å or 3 Å or 2.5 Å or 2 Å or 1.5 Å or 1 Å or 0.5 Å).

We have conducted an rmsd analysis of residue C-α atoms and residue side chain atoms between β1-AR (molecule B) and 62-AR (Cherezov et al, 2007) within the DRY motif (i.e. residues 138-140). The rmsd value for residue C-α atoms is 0.31 Å and for side chain atoms is 0.48 Å. Thus in an embodiment, where the coordinates or selected coordinates used in the invention are optionally varied within the DRY motif, they are varied within an rmsd of C-α atoms of not more than 0.31 Å (such as not more than 0.3 Å or 0.2 Å or 0.1 Å) and/or within an rmsd of side chain atoms of not more than 0.48 Å (such as not more than 0.4 Å or 0.3 Å or 0.2 Å or 0.1 Å).

We have conducted an rmsd analysis of residue backbone atoms and residue side chain atoms between β1-AR (molecule B) and 62-AR (Cherezov et al, 2007) within the residues Val 172 and Phe 325 which are believed to have a profound effect upon ligand binding and specificity. The rmsd value for residue backbone atoms is 0.72 Å and for side chain atoms is 1.99 Å. Thus in an embodiment, where the coordinates or selected coordinates used in the invention are optionally varied within the residues Val 172 and Phe 325, they are varied within an rmsd of residue backbone atoms of not more than 0.72 Å (such as not more than 0.7 Å or 0.6 Å or 0.5 Å or 0.4 Å or 0.3 Å or 0.2 Å or 0.1 Å) and/or within an rmsd of side chain atoms of not more than 1.99 Å (such as not more than 1.9 Å or 1.7 Å or 1.5 Å or 1.3 Å or 1.1 Å or 0.9 Å or 0.7 Å or 0.5 Å or 0.3 Å or 0.1 Å).

We have conducted an rmsd analysis of residue C-α atoms and residue side chain atoms between β1-AR (molecule B) and β2-AR (Cherezov et al, 2007) within the residues Leu 110, Thr 117 and Phe 359 which are thought to be important in ligand specificity. The rmsd value for residue C-α atoms is 0.94 Å and for side chain atoms is 0.92 Å. Thus in an embodiment, where the coordinates or selected coordinates used in the invention are optionally varied within the residues Leu 110, Thr 117 and Phe 359, they are varied within an rmsd of C-α atoms of not more than 0.94 Å (such as not more than 0.9 Å or 0.8 Å or 0.7 Å or 0.6 Å or 0.5 Å or 0.4 Å or 0.3 Å or 0.2 Å or 0.1 Å) and/or within an rmsd of side chain atoms of not more than 0.92 Å (such as not more than 0.9 Å or 0.8 Å or 0.7 Å or 0.6 Å or 0.5 Å or 0.4 Å or 0.3 Å or 0.2 Å or 0.1 Å).

In this aspect of the invention, the coordinates of the turkey β1-AR structure are used to predict a three dimensional representation of a target protein of unknown structure, or part thereof, by modelling. By “modelling”, we mean the prediction of structures using computer-assisted or other de novo prediction of structure, based upon manipulation of the coordinate data from Table A, Table B, Table C or Table D or selected coordinates thereof.

The target protein may be any protein that shares sufficient sequence identity to the turkey β1-AR such that its structure can be modelled by using the turkey β1-AR coordinates of Table A, Table B, Table C or Table D. It will be appreciated that if a structural representation of only a part of the target protein is being modelled, for example a particular domain, the target protein only has to share sufficient sequence identity to the turkey β1-AR over that part.

It has been shown for soluble protein domains that their three dimensional structure is broadly conserved above 20% amino acid sequence identity and well conserved above 30% identity, with the level of structural conservation increasing as amino acid sequence identity increases up to 100% (Ginalski, K. Curr Op Struc Biol (2006) 16, 172-177). Thus, it is preferred if the target protein, or part thereof, shares at least 20% amino acid sequence identity with turkey β1-AR sequence provided in FIG. 7, and more preferably at least 30%, 40%, 50%, 60%, 70%, 80% or 90% sequence identity, and yet more preferably at least 95% or 99% sequence identity.

It will be appreciated therefore that the target protein may be a turkey β1-AR analogue or homologue.

Analogues are defined as proteins with similar three-dimensional structures and/or functions with little evidence of a common ancestor at a sequence level.

Homologues are proteins with evidence of a common ancestor, i.e. likely to be the result of evolutionary divergence and are divided into remote, medium and close sub-divisions based on the degree (usually expressed as a percentage) of sequence identity.

By a turkey β1-AR homologue, we include a protein with at least 20%, 25%, 30%, 35%, 40%, 45% or at least 50% amino acid sequence identity with the sequence of turkey β1-AR provided in FIG. 7, preferably at least 55%, 60%, 65%, 70%, 75% or 80% amino acid sequence identity and more preferably 85%, 90%, 95% or 99% amino acid sequence identity. This includes polymorphic forms of β1-ARs, e.g. mutants and β1-ARs from other species as well as other β-adrenergic receptors such as β2-ARs and β3-ARs. For example, the turkey β1-AR shares 82%, 65% and 58% amino acid sequence identity with human β1-AR, human β2-AR and human β3-AR respectively (when excluding CL3 and N- and C-termini). Thus a turkey β1-AR homologue would include a human β1-AR, a human 32-AR and a human β3-AR.

Sequence identity may be measured by the use of algorithms such as BLAST or PSI-BLAST (Altschul et al, NAR (1997), 25, 3389-3402) or methods based on Hidden Markov Models (Eddy S et al, J Comput Biol (1995) Spring 2 (1) 9-23). Typically, the percent sequence identity between two polypeptides may be determined using any suitable computer program, for example the GAP program of the University of Wisconsin Genetic Computing Group and it will be appreciated that percent identity is calculated in relation to polypeptides whose sequence has been aligned optimally. The alignment may alternatively be carried out using the Clustal W program (Thompson et al., 1994). The parameters used may be as follows: Fast pairwise alignment parameters: K-tuple(word) size; 1, window size; 5, gap penalty; 3, number of top diagonals; 5. Scoring method: x percent. Multiple alignment parameters: gap open penalty; 10, gap extension penalty; 0.05. Scoring matrix: BLOSUM.

In one embodiment the target protein is an integral membrane protein. By “integral membrane protein” we mean a protein that is permanently integrated into the membrane and can only be removed using detergents, non-polar solvents or denaturing agents that physically disrupt the lipid bilayer. Examples include receptors such as GPCRs, the T-cell receptor complex and growth factor, receptors; transmembrane ion channels such as ligand-gated and voltage gated channels; transmembrane transporters such as neurotransmitter transporters; enzymes; carrier proteins; and ion pumps.

The amino acid sequences (and the nucleotide sequences of the cDNAs which encode them) of many membrane proteins are readily available, for example by reference to GenBank. For example, Foord et al supra gives the human gene symbols and human, mouse and rat gene IDs from Entrez Gene (http://www.ncbi.nlm.nih.gov/entrez) for GPCRs. It should be noted, also, that because the sequence of the human genome is substantially complete, the amino acid sequences of human membrane proteins can be deduced therefrom.

In a preferred embodiment, the target protein is a GPCR.

Suitable GPCRs include, but are not limited to β-adrenergic receptors, adenosine receptors, in particular the adenosine A_(2a) receptor, neurotensin receptors (NTR) and muscarinic receptors. Other suitable GPCRs are well known in the art and include those listed in Hopkins & Groom supra. In addition, the International Union of Pharmacology produce a list of GPCRs (Foord et al (2005) Pharmacol. Rev. 57, 279-288, incorporated herein by reference and this list is periodically updated at http://www.iuphar-db.org/GPCR/ReceptorFamiliesForward). It will be noted that GPCRs are divided into different classes, principally based on their amino acid sequence similarities. They are also divided into families by reference to the natural ligands to which they bind. All GPCRs are included in the scope of the invention and their structure may be modelled by using the coordinates of the turkey β1-AR.

Although the target protein may be derived from any source, it is particularly preferred if it is from a eukaryotic source. It is particularly preferred if it is derived from a vertebrate source such as a mammal or a bird. It is particularly preferred if the target protein is derived from rat, mouse, rabbit or dog or non-human primate or man, or from chicken or turkey.

Typically, modelling a structural representation of a target is done by homology modelling whereby homologous regions between the turkey β1-AR and the target protein are matched and the coordinate data of the turkey β1-AR used to predict a structural representation of the target protein.

The term “homologous regions” describes amino acid residues in two sequences that are identical or have similar (e.g. aliphatic, aromatic, polar, negatively charged, or positively charged) side-chain chemical groups. Identical and similar residues in homologous regions are sometimes described as being respectively “invariant” and “conserved” by those skilled in the art.

Typically, the method involves comparing the amino acid sequences of turkey β1-AR with a target protein by aligning the amino acid sequences. Amino acids in the sequences are then compared and groups of amino acids that are homologous (conveniently referred to as “corresponding regions”) are grouped together. This method detects conserved regions of the polypeptides and accounts for amino acid insertions or deletions.

Homology between amino acid sequences can be determined using commercially available algorithms known in the art. For example, the programs BLAST, gapped BLAST, BLASTN, PSI-BLAST, BLAST 2 and WU-BLAST (provided by the National Center for Biotechnology Information) can be used to align homologous regions of two, or more, amino acid sequences. These may be used with default parameters to determine the degree of homology between the amino acid sequence of the turkey β1-AR and other target proteins which are to be modelled.

Preferred for use according to the present invention is the WU-BLAST (Washington University BLAST) version 2.0 software. WU-BLAST version 2.0 executable programs for several UNIX platforms can be downloaded from ftp://blast. wustl. edu/blast/executables. This program is based on WU-BLAST version 1.4, which in turn is based on the public domain NCBI-BLAST version 1.4 (Altschul and Gish, 1996, Local alignment statistics, Doolittle ed., Methods in Enzymology 266: 460-480; Altschul et al., 1990, Basic local alignment search tool, Journal of Molecular Biology 215: 403-410; Gish and States, 1993, Identification of protein coding regions by database similarity search, Nature Genetics 3: 266-272; Karlin and Altschul, 1993, Applications and statistics for multiple high-scoring segments in molecular sequences, Proc. Natl. Acad. Sci. USA 90: 5873-5877; all of which are incorporated by reference herein).

In all search programs in the suite the gapped alignment routines are integral to the database search itself. Gapping can be turned off if desired. The default penalty (O) for a gap of length one is Q=9 for proteins and BLASTP, and Q=10 for BLASTN, but may be changed to any integer. The default per-residue penalty for extending a gap (R) is R=2 for proteins and BLASTP, and R=10 for BLASTN, but may be changed to any integer. Any combination of values for Q and R can be used in order to align sequences so as to maximize overlap and identity while minimizing sequence gaps. The default amino acid comparison matrix is BLOSUM62, but other amino acid comparison matrices such as PAM can be utilized.

Once the amino acid sequences of turkey β1-AR and the target protein of unknown structure have been aligned, the structures of the conserved amino acids in the structural representation of the turkey β1-AR may be transferred to the corresponding amino acids of the target protein. For example, a tyrosine in the amino acid sequence of turkey β1-AR may be replaced by a phenylalanine, the corresponding homologous amino acid in the amino acid sequence of the target protein.

The structures of amino acids located in non-conserved regions may be assigned manually by using standard peptide geometries or by molecular simulation techniques, such as molecular dynamics. The final step in the process is accomplished by refining the entire structure using molecular dynamics and/or energy minimization. Typically, the predicted three dimensional structural representation will be one in which favourable interactions are formed within the target protein and/or so that a low energy conformation is formed (“High resolution structure prediction and the crystallographic phase problem” Qian et al (2007) Nature 450; 259-264; “State of the art in studying protein folding and protein structure production using molecular dynamics methods” Lee et al (2001) J of Mol Graph & Modelling 19(1): 146-149).

Whereas it is preferred to base homology modelling on homologous amino acid sequences, it is appreciated that some proteins have low sequence identity (e.g. family B and C GPCRs) and at the same time are very similar in structure. Therefore, where at least part of the structure of the target protein is known, homologous regions can also be identified by comparing structures directly.

Homology modelling as such is a technique well known in the art (see e.g. Greer, (Science, Vol. 228, (1985), 1055), and Blundell et al (Eur. J. Biochem, Vol. 172, (1988), 513)). The techniques described in these references, as well as other homology modelling techniques generally available in the art, may be used in performing the present invention.

Typically, homology modelling is performed using computer programs, for example SWISS-MODEL available through the Swiss Institute for Bioinformatics in Geneva, Switzerland; WHATIF available on EMBL servers; Schnare et al. (1996) J. Mol. Biol, 256: 701-719; Blundell et al. (1987) Nature 326: 347-352; Fetrow and Bryant (1993) Bio/Technology 11:479-484; Greer (1991) Methods in Enzymology 202: 239-252; and Johnson et al (1994) Crit. Rev. Biochem. Mol. Biol. 29:1-68. An example of homology modelling is described in Szklarz G. D (1997) Life Sci. 61: 2507-2520.

Thus, in an embodiment of the first aspect of the invention, the method further comprises aligning the amino acid sequence of the target protein of unknown structure with the amino acid sequence of turkey β1-AR listed in FIG. 7 to match homologous regions of the amino acid sequences, and subsequently modelling the structural representation of the target protein by modelling the structural representation of the matched homologous regions of the target protein on the corresponding regions of the β1-AR to obtain a three dimensional structural representation for the target protein that substantially preserves the structural representation of the matched homologous regions.

The invention therefore provides a method of predicting a three dimensional structural representation of a target protein of unknown structure, or part thereof, comprising:

-   -   providing the coordinates of the turkey β1-AR structure listed         in Table A, Table B, Table C or Table D, optionally varied by a         root mean square deviation of residue backbone atoms of not more         than 1.235 Å, or selected coordinates thereof; aligning the         amino acid sequence of a target protein of unknown structure or         part thereof with the amino acid sequence of turkey β1-AR listed         in FIG. 7 or part thereof to match homologous regions of the         amino acid sequences;     -   modelling the structure of the matched homologous regions of the         target protein on the corresponding regions of the turkey β1-AR         structure as defined by Table A, Table B, Table C or Table D,         optionally varied by a root mean square deviation of residue         backbone atoms of not more than 1.235 Å, or selected coordinates         thereof; and     -   predicting a three dimensional structural representation for the         target protein which substantially preserves the structure of         the matched homologous regions.

The coordinate data of Table A, Table B, Table C or Table D, or selected coordinates thereof, will be particularly advantageous for homology modelling of other GPCRs. For example, since the protein sequence of β1-AR and dopamine D2 receptor can be aligned relative to each other, it is possible to predict structural representations of the structures of the Dopamine D2 receptor, particularly in the regions of the transmembrane helices and ligand binding region, using the β1-AR coordinates.

The coordinate data of the turkey β1-AR can also be used to predict the crystal structure of target proteins where X-ray diffraction data or NMR spectroscopic data of the protein has been generated and requires interpretation in order to provide a structure.

A second aspect of the invention provides a method of predicting the three dimensional structural representation of a target protein of unknown structure, or part thereof, comprising: providing the coordinates of the turkey β1-AR structure listed in Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof; and either (a) positioning the coordinates in the crystal unit cell of the protein so as to predict its structural representation, or (b) assigning NMR spectra peaks of the protein by manipulating the coordinates.

Thus, where X-ray crystallographic or NMR spectroscopic data is provided for a target protein of unknown structure, the coordinate data of Table A, Table B, Table C or Table D may be used to interpret that data to predict a likely structure using techniques well known in the art including phasing, in the case of X-ray crystallography, and assisting peak assignments in the case of NMR spectra.

A three dimensional structural representation of any part of any target protein that is sufficiently similar to any portion of the turkey β1-AR can be predicted by this method. Typically, the target protein or part thereof has at least 20% amino acid sequence identity with any portion of turkey β1-AR, such as at least 30% amino acid sequence identity or at least 40% or 50% or 60% or 70% or 80% or 90% sequence identity. For example, the coordinates may be used to predict the three-dimensional representations of other crystal forms of turkey β1-AR, other β1-ARs, β1-AR mutants or co-complexes of a β1-AR. Other suitable target proteins are as defined with respect to the first aspect of the invention.

One method that may be employed for these purposes is molecular replacement which is well known in the art and described, for example, in Evans & McCoy (Acta Cryst, 2008, D64:1-10), McCoy (Acta Cryst, 2007, D63:32-42) and McCoy et al (J of App Cryst, 2007, 40:658-674). Molecular replacement enables the solution of the crystallographic phase problem by providing initial estimates of the phases of the new structure from a previously known structure, as opposed to the other major methods for solving the phase problem, i.e. experimental methods (which measure the phase from isomorphous or anomalous differences) or direct methods (which use mathematical relationships between reflection triplets and quartets to bootstrap a phase set for all reflections from phases for a small or random ‘seed’ set of reflections.) Compared to molecular replacement, such methods are time consuming and generally hinder the solution of crystal structures. Thus molecular replacement provides an accurate structural form for an unknown crystal more quickly and efficiently than attempting to determine such information ab initio.

Accordingly, the invention involves generating a preliminary model of a target protein whose structure coordinates are unknown, by orienting and positioning the relevant portion of the turkey β1-AR according to Table A, Table B, Table C or Table D within the unit cell of a crystal of the target protein so as best to account for the observed X-ray diffraction pattern of the crystal of the target protein. Phases can be calculated from this model and combined with the observed X-ray diffraction pattern amplitudes to generate an electron density map of the target protein's structure. This, in turn, can be subjected to any well-known model building and structure refinement techniques to provide a final, accurate structural representation of the target protein (E. Lattman, “Use of the Rotation and Translation Functions”, in Meth. Enzymol., 115, pp. 55-77 (1985); M. G. Rossmann, ed., “The Molecular Replacement Method”, Int. Sci. Rev. Ser., No. 13, Gordon & Breach, New York (1972)).

Thus the invention includes a method of predicting a three dimensional structural representation of a target protein of unknown structure, or part thereof, comprising: providing the coordinates of the turkey β1-AR structure, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof; providing an X-ray diffraction pattern of the target protein; and using the coordinates to predict at least part of the structure coordinates of the target protein.

In an embodiment, the X-ray diffraction pattern of the target protein is provided by crystallising the target protein unknown structure; and generating an X-ray diffraction pattern from the crystallised target protein. Thus, the invention also provides a method of method of predicting a three dimensional structural representation of a target protein of unknown structure comprising the steps of (a) crystallising the target protein; (b) generating an X-ray diffraction pattern from the crystallised target protein; (c) applying the coordinates of the turkey β1-AR structure, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof, to the X-ray diffraction pattern to generate a three-dimensional electron density map of the target protein, or part thereof; and (d) predicting a three dimensional structural representation of the target protein from the three-dimensional electron density map.

Examples of computer programs known in the art for performing molecular replacement include CNX (Brunger A T.; Adams P. D.; Rice L. M., Current Opinion in Structural Biology, Volume 8, Issue 5, October 1998, Pages 606-611 (also commercially available from Accelrys San Diego, Calif.), MOLREP (A. Vagin, A. Teplyakov, MOLREP: an automated program for molecular replacement, J Appl Cryst (1997) 30, 1022-1025, part of the CCP4 suite) or AMoRe (Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Cryst A50, 157-163).

Preferred selected coordinates of the turkey β1-AR are as defined above with respect to the first aspect of the invention.

The invention may also be used to assign peaks of NMR spectra of target proteins, by manipulation of the data of Table A, Table B, Table C or Table D (J Magn Reson (2002) 157(1): 119-23).

The coordinates of the β1-AR of Table A, Table B, Table C or Table D optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof may be used in the provision, design, modification or analysis of binding partners of β1-ARs. Such a use will be important in drug design.

By β1-AR we mean any β1-AR which has at least 75% sequence identity with turkey β1-AR, including turkey β1-AR as well as β1-AR from other species and mutants thereof. For example, human β1-AR has 82% amino acid sequence identity with turkey β1-AR. Therefore it is preferred if the β1-AR has at least 82% amino acid sequence identity to turkey β1-AR, more preferably at least 85%, 90%, 95% or 99% amino acid sequence identity.

By “binding partner” we mean any molecule that binds to a β1-AR. Preferably, the molecule binds selectively to the β1-AR. For example, it is preferred if the binding partner has a K_(d) value (dissociation constant) which is at least five or ten times lower (i.e. higher affinity) than for at least one other β-AR (e.g. β2-AR or β3-AR), and preferably more than 100 or 500 times lower. More preferably, the binding partner of a β1-AR has a K_(d) value more than 1000 or 5000 times lower than for at least one other β-AR. However, it will be appreciated that the limits will vary dependent upon the nature of the binding partner. Thus, typically, for small molecule binding partners, the binding partner typically has a K_(d) value which is at least 50 times or 100 times lower than for at least one other β-AR. Typically, for antibody binding partners, the binding partner typically has a K_(d) value which is at least 500 or 1000 times lower than for at least one other β-AR.

K_(d) values can be determined readily using methods well known in the art and as described, for example, below.

At equilibrium Kd=[R][L]/[RL]

where the terms in brackets represent the concentration of

-   -   Receptor-ligand complexes [RL],     -   unbound receptor [R], and     -   unbound (“free”) ligand [L].

In order to determine the K_(d) the value of these terms must be known. Since the concentration of receptor is not usually known then the Hill-Langmuir equation is used where

Fractional occupancy=[L]/[L]+K _(d).

In order to experimentally determine a K_(d) then, the concentration of free ligand and bound ligand at equilibrium must be known. Typically, this can be done by using a radio-labelled or fluorescently labelled ligand which is incubated with the receptor (present in whole cells or homogenised membranes) until equilibrium is reached. The amount of free ligand vs bound ligand must then be determined by separating the signal from bound vs free ligand. In the case of a radioligand this can be done by centrifugation or filtration to separate bound ligand present on whole cells or membranes from free ligand in solution. Alternatively a scintillation proximity assay is used. In this assay the receptor (in membranes) is bound to a bead containing scintillant and a signal is only detected by the proximity of the radioligand bound to the receptor immobilised on the bead.

The binding partner may be any of a polypeptide; an anticalin; a peptide; an antibody; a chimeric antibody; a single chain antibody; an aptamer; a darpin; a Fab, F(ab′)₂, Fv, ScFv or dAb antibody fragment; a small molecule; a natural product; an affibody; a peptidomimetic; a nucleic acid; a peptide nucleic acid molecule; a lipid; a carbohydrate; a protein based on a modular framework including ankyrin repeat proteins, armadillo repeat proteins, leucine rich proteins, tetrariopeptide repeat proteins or Designed Ankyrin Repeat Proteins (DARPins); a protein based on lipocalin or fibronectin domains or Affilin scaffolds based on either human gamma crystalline or human ubiquitin; a G protein; an RGS protein; an arrestin; a GPCR kinase; a receptor tyrosine kinase; a RAMP; a NSF; a GPCR; an NMDA receptor subunit NR1 or NR2a; calcyon; or a fragment or derivative thereof that binds to β1-AR.

It will be appreciated that the coordinates of the invention will also be useful in the analysis of solvent and ion interactions with a β1-AR, which are important factors in drug design. Thus the binding partner may be a solvent molecule, for example water or acetonitrile, or an ion, for example a sodium ion or a protein.

It is particularly preferred if the binding partner is a small molecule with a molecule weight less than 5000 daltons, for example less than 4000, 3000, 2000 or 1000 daltons, or with a molecule weight less than 500 daltons, for example less than 450 daltons, 400 daltons, 350 daltons, 300 daltons, 250 daltons, 200 daltons, 150 daltons, 100 daltons, 50 daltons or 10 daltons.

It is further preferred if the binding partner causes a change (i.e a modulation) in the level of biological activity of the β1-AR, i.e. it has functional agonist or antagonist activity, and therefore may have the potential to be a candidate drug. Thus, the binding partner may be any of a full agonist, a partial agonist, an inverse agonist or an antagonist of β1-AR.

Accordingly, a third aspect of the invention provides a method for selecting or designing one or more binding partners of β1-AR comprising using molecular modelling means to select or design one or more binding partners of β1-AR, wherein the three-dimensional structural representation of at least part of turkey β1-AR, as defined by the coordinates of turkey β1-AR of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å or selected coordinates thereof, is compared with a three-dimensional structural representation of one or more candidate binding partners, and one or more binding partners that are predicted to interact with β1-AR are selected.

In order to provide a three-dimensional structural representation of a candidate binding partner, the binding partner structural representation may be modelled in three dimensions using commercially available software for this purpose or, if its crystal structure is available, the coordinates of the structure may be used to provide a structural representation of the binding partner.

The design of binding partners that bind to a β1-AR generally involves consideration of two factors.

First, the binding partner must be capable of physically and structurally associating with parts or all of a β1-AR binding region. Non-covalent molecular interactions important in this association include hydrogen bonding, van der Waals interactions, hydrophobic interactions and electrostatic interactions.

Second, the binding partner must be able to assume a conformation that allows it to associate with a β1-AR binding region directly. Although certain portions of the binding partner will not directly participate in these associations, those portions of the binding partner may still influence the overall conformation of the molecule. This, in turn, may have a significant impact on potency. Such conformational requirements include the overall three-dimensional structure and orientation of the binding partner in relation to all or a portion of the binding region, or the spacing between functional groups of a binding partner comprising several binding partners that directly interact with the β1-AR.

Thus it will be appreciated that selected coordinates which represent a binding region of the turkey β1-AR, e.g. atoms from amino acid residues contributing to the ligand binding site including amino acid residues 117, 118, 121, 122, 125, 201, 203, 207, 211, 215, 306, 307, 310 and 329 and amino acid residues 172 and 325 may be used. Selected coordinates representing an extracellular face would be useful to select or design for antibodies, and selected coordinates representing an intracellular face would be useful to select or design for natural binding partners such as G proteins.

Additional preferences for the selected coordinates are as defined above with respect to the first aspect of the invention.

Designing of binding partners can generally be achieved in two ways, either by the step wise assembly of a binding partner or by the de novo synthesis of a binding partner.

With respect to the step-wise assembly of a binding partner, several methods may be used. Typically the process begins by visual inspection of, for example, any of the binding regions on a computer representation of the turkey β1-AR as defined by the coordinates in Table A, Table B, Table C or Table D optionally varied within a rmsd of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof. Selected binding partners, or fragments or moieties thereof may then be positioned in a variety of orientations, or docked, within the binding region. Docking may be accomplished using software such as QUANTA and Sybyl (Tripos Associates, St. Louis, Mo.), followed by, or performed simultaneously with, energy minimization, rigid-body minimization (Gshwend, supra) and molecular dynamics with standard molecular mechanics force fields, such as CHARMM and AMBER.

Specialized computer programs may also assist in the process of selecting binding partners or fragments or moieties thereof. These include: 1. GRID (P. J. Goodford, “A Computational Procedure for Determining Energetically Favorable Binding Sites on Biologically Important Macromolecules”, J. Med. Chem., 28, pp. 849-857 (1985)). GRID is available from Oxford University, Oxford, UK. 2. MCSS (A. Miranker et al., “Functionality Maps of Binding Sites: A Multiple Copy Simultaneous Search Method.”Proteins: Structure, Function and Genetics, 11, pp. 29-34 (1991)). MCSS is available from Molecular Simulations, San Diego, Calif. 3. AUTODOCK (D. S. Goodsell et al., “Automated Docking of Substrates to Proteins by Simulated Annealing”, Proteins: Structure, Function, and Genetics, 8, pp. 195-202 (1990)). AUTODOCK is available from Scripps Research Institute, La Jolla, Calif. 4. DOCK (I. D. Kuntz et al., “A Geometric Approach to Macromolecule-Ligand Interactions”, J. Mol. Biol., 161, pp. 269-288 (1982)). DOCK is available from University of California, San Francisco, Calif.

Once suitable binding partners or fragments have been selected, they may be assembled into a single compound or complex. Assembly may be preceded by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates of the turkey β1-AR. This would be followed by manual model building using software such as QUANTA or Sybyl.

Useful programs to aid one of skill in the art in connecting the individual chemical entities or fragments include: 1. CAVEAT (P. A. Bartlett et al., “CAVEAT: A Program to Facilitate the Structure-Derived Design of Biologically Active Molecules”, in “Molecular Recognition in Chemical and Biological Problems”, Special Pub., Royal Chem. Soc., 78, pp. 182-196 (1989); G. Lauri and P. A. Bartlett, “CAVEAT: a Program to Facilitate the Design of Organic Molecules”, J. Comput. Aided Mol. Des., 8, pp. 51-66 (1994)). CAVEAT is available from the University of California, Berkeley, Calif.; 2. 3D Database systems such as ISIS (MDL Information Systems, San Leandro, Calif.). This area is reviewed in Y. C. Martin, “3D Database Searching in Drug Design”, J. Med. Chem., 35, pp. 2145-2154 (1992); and 3. HOOK (M. B. Eisen et al., “HOOK: A Program for Finding Novel Molecular Architectures that Satisfy the Chemical and Steric Requirements of a Macromolecule Binding Site”, Proteins: Struct., Funct., Genet., 19, pp. 199-221 (1994). HOOK is available from Molecular Simulations, San Diego, Calif.

Thus the invention includes a method of designing a binding partner of a β1-AR comprising the steps of: (a) providing a structural representation of a β1-AR binding region as defined by the coordinates of turkey β1-AR of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å or selected coordinates thereof (b) using computational means to dock a three dimensional structural representation of a first binding partner in part of the binding region; (c) docking at least a second binding partner in another part of the binding region; (d) quantifying the interaction energy between the first or second binding partner and part of the binding region; (e) repeating steps (b) to (d) with another first and second binding partner, selecting a first and a second binding partner based on the quantified interaction energy of all of said first and second binding partners; (f) optionally, visually inspecting the relationship of the first and second binding partner to each other in relation to the binding region; and (g) assembling the first and second binding partners into a one binding partner that interacts with the binding region by model building.

As an alternative to the step-wise assembly of binding partners, binding partners may be designed as a whole or “de novo” using either an empty binding region or optionally including some portion(s) of a known binding partner(s). There are many de novo ligand design methods including: 1. LUDI (H.-J. Bohm, “The Computer Program LUDI: A New Method for the De Novo Design of Enzyme Inhibitors”, J. Comp. Aid. Molec. Design, 6, pp. 61-78 (1992)). LUDI is available from Molecular Simulations Incorporated, San Diego, Calif.; 2. LEGEND (Y. Nishibata et al., Tetrahedron, 47, p. 8985 (1991)). LEGEND is available from Molecular Simulations Incorporated, San Diego, Calif.; 3. LeapFrog (available from Tripos Associates, St. Louis, Mo.); and 4. SPROUT (V. Gillet et al., “SPROUT: A Program for Structure Generation)”, J. Comput. Aided Mol. Design, 7, pp. 127-153 (1993)). SPROUT is available from the University of Leeds, UK.

Other molecular modelling techniques may also be employed in accordance with this invention (see, e.g., N. C. Cohen et al., “Molecular Modeling Software and Methods for Medicinal Chemistry, J. Med. Chem., 33, pp. 883-894 (1990); see also, M. A. Navia and M. A. Murcko, “The Use of Structural Information in Drug Design”, Current Opinions in Structural Biology, 2, pp. 202-210 (1992); L. M. Balbes et al., “A Perspective of Modern Methods in Computer-Aided Drug Design”, in Reviews in Computational Chemistry, Vol. 5, K. B. Lipkowitz and D. B. Boyd, Eds., VCH, New York, pp. 337-380 (1994); see also, W. C. Guida, “Software For Structure-Based Drug Design”, Curr. Opin. Struct. Biology, 4, pp. 777-781 (1994)).

In addition to the methods described above in relation to the design of binding partners, other computer-based methods are available to select for binding partners that interact with β1-AR.

For example the invention involves the computational screening of small molecule databases for binding partners that can bind in whole, or in part, to the turkey β1-AR.

In this screening, the quality of fit of such binding partners to a binding region of a β1-AR site as defined by the coordinates of turkey β1-AR of Table A, Table B, Table. C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å or selected coordinates thereof, may be judged either by shape complementarity or by estimated interaction energy (E. C. Meng et. al., J. Comp. Chem., 13, pp. 505-524 (1992)).

For example, selection may involve using a computer for selecting an orientation of a binding partner with a favourable shape complementarity in a binding region comprising the steps of: (a) providing the coordinates of turkey β1-AR of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å or selected coordinates thereof and a three-dimensional structural representation of one or more candidate binding partners; (b) employing computational means to dock a first binding partner in the binding region; (c) quantitating the contact score of the binding partner in different orientions; and (d) selecting an orientation with the highest contact score.

The docking may be facilitated by the contact score. The method may further comprise the step of generating a three-dimensional structural repsentation of the binding region and binding partner bound therein prior to step (b).

The method may further comprise the steps of: (e) repeating steps (b) through (d) with a second binding partner; and (f) selecting at least one of the first or second binding partner that has a higher contact score based on the quantitated contact score of the first or second binding partner.

In another embodiment, selection may involve using a computer for selecting an orientation of a binding partner that interacts favourably with a binding region comprising; a) providing the coordinates of turkey β1-AR of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å or selected coordinates thereof; b) employing computational means to dock a first binding partner in the binding region; c) quantitating the interaction energy between the binding partner and all or part of a binding region for different orientations of the binding partner; and d) selecting the orientation of the binding partner with the most favorable interaction energy.

The docking may be facilitated by the quantitated interaction energy and energy minimization with or without molecular dynamics simulations may be performed simultaneously with or following step (b).

The method may further comprise the steps of: (e) repeating steps (b) through (d) with a second binding partner; and (f) selecting at least one of the first or second binding partner that interacts more favourably with a binding region based on the quantitated interaction energy of the first or second binding partner.

In another embodiment, selection may involve screening a binding partner to associate at a deformation energy of binding of less than −7 kcal/mol with a β1-AR binding region comprising: (a) providing the coordinates of turkey rβ1-AR of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å or selected coordinates thereof and employing computational means which utilise coordinates to dock the binding partner into a binding region; (b) quantifying the deformation energy of binding between the binding partner and the binding region; and (d) selecting a binding partner that associates with a β1-AR binding region at a deformation energy of binding of less than −7 kcal/mol.

It is appreciated that in some instances high throughput screening of binding partners is preferred and that methods of the invention may be used as “library screening” methods, a term well known to those skilled in the art. Thus, the binding partner may be a library of binding partners. For example, the library may be a peptide or protein library produced, for example, by ribosome display or an antibody library prepared either in vivo, ex vivo or in vitro. Methodologies for preparing and screening such libraries are known in the art.

Determination of the three-dimensional structure of the turkey β1-AR provides important information about the binding sites of β1-ARs, particularly when comparisons are made with other β-ARs. This information may then be used for rational design and modification of β1-AR binding partners, e.g. by computational techniques which identify possible binding ligands for the binding sites, by enabling linked-fragment approaches to drug design, and by enabling the identification and location of bound ligands using X-ray crystallographic analysis. These techniques are discussed in more detail below.

Thus as a result of the determination of the turkey β1-AR three-dimensional structure, more purely computational techniques for rational drug design may also be used to design structures whose interaction with β1-AR is better understood (for an overview of these techniques see e.g. Walters et al (Drug Discovery Today, Vol. 3, No. 4, (1998), 160-178; Abagyan, R.; Totrov, M. Curr. Opin. Chem. Biol. 2001, 5, 375-382). For example, automated ligand-receptor docking programs (discussed e.g. by Jones et al. in Current Opinion in Biotechnology, Vol. 6, (1995), 652-656 and Halperin, I.; Ma, B.; Wolfson, H.; Nussinov, R. Proteins 2002, 47, 409-443), which require accurate information on the atomic coordinates of target receptors may be used.

The aspects of the invention described herein which utilize the β1-AR structure in silico may be equally applied to both the turkey β1-AR structure of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof; and predicting the three-dimensional structural representation of the target protein, or part thereof, by modelling the structural representation on all or the selected coordinates of the turkey β1-AR or selected coordinates thereof and the models of target proteins obtained by the first and second aspects of the invention. Thus having determined a conformation of a target protein, for example a β1-AR, by the methods described above, such a conformation may be used in a computer-based method of rational drug design as described herein. In addition, the availability of the structure of the turkey β1-AR will allow the generation of highly predictive pharmacophore models for virtual library screening or ligand design.

Accordingly, a fourth aspect of the invention provides a method for the analysis of the interaction of one or more binding partners with β1-AR, comprising: providing a three dimensional structural representation of β1-AR as defined by the coordinates of the turkey β1-AR structure of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof; providing a three dimensional structural representation of one or more binding partners to be fitted to the structural representation of β1-AR or selected coordinates thereof; and fitting the one of more binding partners to said structure.

This method of the invention is generally applicable for the analysis of known binding partners of β1-AR, the development or discovery of binding partners of β1-AR, the modification of binding partners of β1-AR e.g. to improve or modify one or more of their properties, and the like. Moreover, the methods of the invention are useful in identifying binding partners than are selective for β1-ARs over β2-ARs. For example, comparing corresponding binding regions between β1-AR and β2-AR will facilitate the design of β1-AR specific binding partners.

It will be desirable to model a sufficient number of atoms of the β1-AR as defined by the coordinates of Table A, Table B, Table C or Table D optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof, which represent a binding region, e.g. atoms from amino acid residues contributing to the ligand binding site including amino acid residues 117, 118, 121, 122, 125, 201, 203, 207, 211, 215, 306, 307, 310 and 329. Although every different binding partner bound by β1-AR may interact with different parts of the binding region of the protein, the structure of the turkey β1-AR allows the identification of a number of particular sites which are likely to be involved in many of the interactions of β1-AR with a drug candidate. Additional preferred selected coordinates are as described as above with respect to the first aspect of the invention.

In order to provide a three-dimensional structural representation of a binding partner to be fitted to the turkey β1-AR structure, the binding partner structural representation may be modelled in three dimensions using commercially available software for this purpose or, if its crystal structure is available, the coordinates of the structure may be used to provide a structural representation of the binding partner for fitting to the turkey β1-AR structure of the invention.

By “fitting”, is meant determining by automatic, or semi-automatic means, interactions between one or more atoms of a candidate binding partner and at least one atom of the turkey β1-AR structure of the invention, and calculating the extent to which such interactions are stable. Interactions include attraction and repulsion, brought about by charge, steric, lipophilic, considerations and the like. Charge and steric interactions of this type can be modelled computationally. An example of such computation would be via a force field such as Amber (Cornell et al., A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic Molecules, Journal of the American Chemical Society, (1995), 117(19), 5179-97) which would assign partial charges to atoms on the protein and binding partner and evaluate the electrostatic interaction energy between a protein and binding partner atom using the Coulomb potential. The Amber force field would also assign van der Waals energy terms to assess the attractive and repulsive steric interactions between two atoms. Lipophilic interactions can be modeled using a variety of means. For example the ChemScore function (Eldridge M D; Murray C W; Auton T R; Paolini G V; Mee R P Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of binding partners in receptor complexes, Journal of computer-aided molecular design (1997 September), 11 (5), 425-45) assigns protein and binding partner atoms as hydrophobic or polar, and a favourable energy term is specified for the interaction between two hydrophobic atoms. Other methods of assessing the hydrophobic contributions to ligand binding are available and these would be known to one skilled in the art. Other methods of assessing interactions are available and would be known to one skilled in the art of designing molecules. Various computer-based methods for fitting are described further herein.

More specifically, the interaction of a binding partner with the turkey β1-AR structure of the invention can be examined through the use of computer modelling using a docking program such as GOLD (Jones et al., J. Mol. Biol., 245, 43-53 (1995), Jones et al., J. Mol. Biol., 267, 727-748 (1997)), GRAMM (Vakser, I. A., Proteins, Suppl., 1: 226-230 (1997)), DOCK (Kuntz et al, (1982) J. Mol. Biol., 161, 269-288; Makino et al, (1997) J. Comput. Chem., 18, 1812-1825), AUTODOCK (Goodsell et al, (1990) Proteins, 8, 195-202, Morris et al, (1998) J. Comput. Chem., 19, 1639-1662.), FlexX, (Rarey et al, (1996) J. Mol. Biol., 261, 470-489) or ICM (Abagyan et al, (1994) J. Comput. Chem., 15, 488-506). This procedure can include computer fitting of binding partners to the turkey β1-AR structure to ascertain how well the shape and the chemical structure of the binding partner will bind to a β1-AR.

Thus the invention includes a method for the analysis of the interaction of one or more binding partners with β1-AR comprising (a) constructing a computer representation of a binding region of the turkey β1-AR as defined by the coordinates of turkey β1-AR of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å or selected coordinates thereof (b) selecting a binding partner to be evaluated by a method selected from the group consisting of assembling said binding partner; selecting a binding partner from a small molecule database; de novo ligand design of the binding partner; and modifying a known agonist or inhibitor, or a portion thereof, of a β1-AR or homologue thereof; (c) employing computational means to dock said binding partner to be evaluated in a binding region in order to provide an energy-minimized configuration of the binding partner in a binding region; and (d) evaluating the results of said docking to quantify the interaction energy between said, binding partner and the binding region.

Also computer-assisted, manual examination of the binding region structure of the turkey β1-AR may be performed. The use of programs such as GRID (Goodford, (1985) J. Med. Chem., 28, 849-857)—a program that determines probable interaction sites between molecules with various functional groups and an enzyme surface—may also be used to analyse a binding region to predict, for example, the types of modifications which will alter the rate of metabolism of a binding partner.

Computer programs can be employed to estimate the attraction, repulsion, and steric hindrance of the turkey β1-AR structure and a binding partner.

If more than one turkey β1-AR binding region is characterized and a plurality of respective smaller molecular fragments are designed or selected, a binding partner may be formed by linking the respective small molecular fragments into a single binding partner, which maintains the relative positions and orientations of the respective small molecular fragments at the binding sites. The single larger binding partner may be formed as a real molecule or by computer modelling. Detailed structural information can then be obtained about the binding of the binding partner to β1-AR, and in the light of this information adjustments can be made to the structure or functionality of the binding partner, e.g. to alter its interaction with β1-AR. The above steps may be repeated and re-repeated as necessary.

Thus, the three dimensional structural representation of the one or more binding partners of the third and fourth aspects of the invention may be obtained by: providing structural representations of a plurality of molecular fragments; fitting the structural representation of each of the molecular fragments to the coordinates of the turkey β1-AR structural representation of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue C-α atoms of not more than 1.235 Å, or selected coordinates thereof; and assembling the representations of the molecular fragments into one or more representations of single molecules to provide the three-dimensional structural representation of one or more candidate binding partners.

Typically the binding partner or molecule fragment is fitted to at least 5 or 10 non-hydrogen atoms of the turkey β1-AR structure, preferably at least 20, 30, 40, 50, 60, 70, 80 or 90 non-hydrogen atoms and more preferably at least 100, 150, 200, 250, 300, 350, 400, 450, or 500 atoms and even more preferably at least 600, 700, 800, 900, 1000, 1100, 1200, 1300, 1400, 1500, 1600, 1700, 1800, 1900, 2000, 2100 or 2200 non-hydrogen atoms.

The invention includes screening methods to identify drugs or lead compounds of use in treating a disease or condition. For example, large numbers of binding partners, for example in a chemical database, can be screened for their ability to bind β1-AR.

It is appreciated that in the methods described herein, which may be drug screening methods, a term well known to those skilled in the art, the binding partner may be a drug-like compound or lead compound for the development of a drug-like compound.

The term “drug-like compound” is well known to those skilled in the art, and may include the meaning of a compound that has characteristics that may make it suitable for use in medicine, for example as the active ingredient in a medicament. Thus, for example, a drug-like compound may be a molecule that may be synthesised by the techniques of organic chemistry, less preferably by techniques of molecular biology or biochemistry, and is preferably a small molecule, which may be of less than 5000 daltons (such as less than 560 daltons) and which may be water-soluble. A drug-like compound may additionally exhibit features of selective interaction with a particular protein or proteins and be bioavailable and/or able to penetrate target cellular membranes or the blood:brain barrier, but it will be appreciated that these features are not essential.

The term “lead compound” is similarly well known to those skilled in the art, and may include the meaning that the compound, whilst not itself suitable for use as a drug (for example because it is only weakly potent against its intended target, non-selective in its action, unstable, poorly soluble, difficult to synthesise or has poor bioavailability) may provide a starting-point for the design of other compounds that may have more desirable characteristics.

Thus in one embodiment of the methods of third and fourth aspects of the invention, the methods further comprise modifying the structural representation of the binding partner so as to increase or decrease their interaction with β1-AR.

For example, once a binding partner has been designed or selected by the above methods, the efficiency with which that binding partner may bind to a β1-AR may be tested and optimized, for example by computational evaluation. For example, a binding partner designed or selected as binding to a β1-AR may be further computationally optimized so that in its bound state it would preferably lack repulsive electrostatic interaction with the target β1-AR and with the surrounding water molecules. Such non-complementary electrostatic interactions include repulsive charge-charge, dipole-dipole and charge-dipole interactions.

Furthermore, it is often desired that binding partners demonstrate a relatively small difference in energy between the bound and free states (i.e., a small deformation energy of binding). Thus, binding partners may be designed with a deformation energy of binding of not greater than about 10 kcal/mole, more preferably, not greater than 7 kcal/mole. Binding partners may interact with the binding region in more than one conformation that is similar in overall binding energy. In those cases, the deformation energy of binding is taken to be the difference between the energy of the free binding partner and the average energy of the conformations observed when the binding partner binds to the protein.

Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interactions. Examples of programs designed for such uses include: Gaussian 94, revision C (M. J. Frisch, Gaussian, Inc., Pittsburgh, Pa. .COPYRGT. 1995); AMBER, version 4.1 (P. A. Kollman, University of California at San Francisco, .COPYRGT. 1995); QUANTA/CHARMM (Molecular Simulations, Inc., San Diego, Calif. COPYRGT. 1998); Insight II/Discover (Molecular Simulations, Inc., San Diego, Calif. COPYRGT. 1998); DelPhi (Molecular Simulations, Inc., San Diego, Calif. COPYRGT. 1998); and AMSOL (Quantum Chemistry Program Exchange, Indiana University). These programs may be implemented, for instance, using a Silicon Graphics workstation such as an Indigo2 with “IMPACT” graphics. Other hardware systems and software packages will be known to those skilled in the art.

By modifying the structural representation we include, for example, adding molecular scaffolding, adding or varying functional groups, or connecting the molecule with other molecules (e.g. using a fragment linking approach) such that the chemical structure of the binding partner is changed while its original binding to β1-AR capability is increased or decreased. Such optimisation is regularly undertaken during drug development programmes to e.g. enhance potency, promote pharmacological acceptability, increase chemical stability etc. of lead compounds.

Examples of modifications include substitutions or removal of groups containing residues which interact with the amino acid side chain groups of the β1-AR structure of the invention. For example, the replacements may include the addition or removal of groups in order to decrease or increase the charge of a group in a binding partner, the replacement of a charge group with a group of the opposite charge, or the replacement of a hydrophobic group with a hydrophilic group or vice versa. It will be understood that these are only examples of the type of substitutions considered by medicinal chemists in the development of new pharmaceutical compounds and other modifications may be made, depending upon the nature of the starting binding partner and its activity.

The potential binding effect of a binding partner on β1-AR may be analysed prior to its actual synthesis and testing by the use of computer modeling techniques. If the theoretical structure of the given entity suggests insufficient interaction and association between it and the β1-AR, testing of the entity is obviated. However, if computer modelling indicates a strong interaction, the molecule may then be synthesized and tested for its ability to bind to a β1-AR. In this manner, synthesis of inoperative compounds may be avoided.

Thus in a further embodiment of the third and fourth aspects of the invention, the methods further comprise the steps of obtaining or synthesising the one or more binding partners of a β1-AR; and optionally contacting the one or more binding partners with a β1-AR to determine the ability of the one or more binding partners to interact with the β1-AR.

Various methods may be used to determine binding between a β1-AR and a binding partner including, for example, enzyme linked immunosorbent assays (ELISA), surface plasmon resonance assays, chip-based assays, immunocytofluorescence, yeast two-hybrid technology and phage display which are common practice in the art and are described, for example, in Plant et al (1995) Analyt Biochem, 226(2), 342-348 and Sambrook et al (2001) Molecular Cloning A Laboratory Manual. Third Edition. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. Other methods of detecting binding, between a β1-AR and a binding partner include ultrafiltration with ion spray mass spectroscopy/HPLC methods or other physical and analytical methods. Fluorescence Energy Resonance Transfer (FRET) methods, for example, well known to those skilled in the art, may be used, in which binding of two fluorescent labelled entities may be measured by measuring the interaction of the fluorescent labels when in close proximity to each other.

Once computer modelling has indicated that a binding partner has a strong interaction, it is appreciated that it may be desirable to crystallise a complex of the β1-AR with that binding partner and analyse its interaction further by X-ray crystallography.

Thus in a further embodiment of the third and fourth aspects of the invention, the methods further comprise the steps of obtaining or synthesising the one or more binding partners of a β1-AR; forming one or more complexes of the β1-AR and the one or more binding partners; and analysing the one or more complexes by X-ray crystallography to determine the ability of the one or more binding partners to interact with β1-AR.

Thus, it will be appreciated that another particularly useful drug design technique enabled by this invention is iterative drug design. Iterative drug design is a method for optimizing associations between a protein and a binding partner by determining and evaluating the three-dimensional structures of successive sets of protein/compound complexes.

In iterative drug design, crystals of a series of proteins or protein complexes are obtained and then the three-dimensional structures of each crystal is solved. Such an approach provides insight into the association between the proteins and binding partners of each complex. This is accomplished by selecting candidate binding partners, obtaining crystals of this new protein/binding partner complex, solving the three-dimensional structure of the complex, and comparing the associations between the new protein/binding partner complex and previously solved protein/binding partner complexes. By observing how changes in the binding partner affected the protein/binding partner associations, these associations may be optimized.

In some cases, iterative drug design is carried out by forming successive protein-binding partner complexes and then crystallizing each new complex. High throughput crystallization assays may be used to find a new crystallization condition or to optimize the original protein or complex crystallization condition for the new complex. Alternatively, a pre-formed protein crystal may be soaked in the presence of a binding partner, thereby forming a protein/binding partner complex and obviating the need to crystallize each individual protein/binding partner complex.

The ability of a binding partner to modify β1-AR function may also be tested. For example the ability of a binding partner to modulate a β1-AR function could be tested by a number of well known standard methods, described extensively in the prior art.

In addition to in silico analysis and design, the interaction of one or more binding partners with a β1-AR may be analysed directly by X-ray crystallography experiments, wherein the coordinates of the turkey β1-AR of Table A, Table B, Table C or Table D optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof, are used to analyse the a crystal complex of the β1-AR and binding partner. This can provide high resolution information of the interaction and can also provide insights into a mechanism by which a binding partner exerts an agonistic or antagonistic function.

Accordingly, a fifth aspect of the invention provides a method for the analysis of the interaction of one or more binding partners with β1-AR, comprising: obtaining or synthesising one or more binding partners; forming one or more crystallised complexes of a β1-AR and a binding partner; and analysing the one or more complexes by X-ray crystallography by employing the coordinates of the turkey β1-AR structure, of Table A, Table B, Table C or Table D optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof, to determine the ability of the one or more binding partners to interact with the β1-AR.

Preferences for the selected coordinates in this and all subsequent aspects of the invention are as defined above with respect to the first aspect of the invention.

The analysis of such structures may employ X-ray crystallographic diffraction data from the complex and the coordinates of the turkey β1-AR structure, of Table A, Table B, Table C or Table D optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof, to generate a difference Fourier electron density map of the complex. The difference Fourier electron density map may then be analysed.

In one embodiment, the one or more crystallised complexes are formed by soaking a crystal of β1-AR with the binding partner to form a complex. Alternatively, the complexes may be obtained by cocrystallising the β1-AR with the binding partner. For example a purified β1-AR protein sample is incubated over a period of time (usually >1 hr) with a potential binding partner and the complex can then be screened for crystallization conditions. Alternatively, protein crystals containing a first binding partner can be back-soaked to remove this binding partner by placing the crystals into a stabilising solution in which the binding partner is not present. The resultant crystals can then be transferred into a second solution containing a second binding partner and used to produce an X-ray diffraction pattern of β1-AR complexed with the second binding partner.

The complexes can be analysed using X-ray diffraction methods, e.g. according to the approach described by Greer et al., (J of Medicinal Chemistry, Vol. 37, (1994), 1035-1054), and difference Fourier electron density maps can be calculated based on X-ray diffraction patterns of soaked or co-crystallized β1-AR and the solved structure of uncomplexed β1-AR. These maps can then be analysed e.g. to determine whether and where a particular ligand binds to β1-AR and/or changes the conformation of β1-AR.

Electron density maps can be calculated using programs such as those from the CCP4 computing package (Collaborative Computational Project 4. The CCP4 Suite: Programs for Protein Crystallography, Acta Crystallographica, D50, (1994), 760-763.). For map visualization and model building programs such as “0” (Jones et al., Acta Crystallographica, A47, (1991), 110-119) can be used.

All of the complexes referred to above may be studied using well-known X-ray diffraction techniques and may be refined against 1.5 to 3.5 A resolution X-ray data to an R value of about 0.30 or less using computer software, such as CNX (Brunger et al., Current Opinion in Structural Biology, Vol. 8, Issue 5, October 1998, 606-611, and commercially available from Accelrys, San Diego, Calif.)1 and as described by Blundell et al, (1976) and Methods in Enzymology, vol. 114 & 115, H. W. Wyckoff et al., eds., Academic Press (1985).

This information may thus be used to optimise known classes of β1-AR binding partners and to design and synthesize novel classes of β1-AR binding partners, particularly those which have agonistic or antagonistic properties, and to design drugs with modified β1-AR interactions.

In one approach, the structure of a binding partner bound to a β1-AR may be determined by experiment. This will provide a starting point in the analysis of the binding partner bound to β1-AR thus providing those of skill in the art with a detailed insight as to how that particular binding partner interacts with β1-AR and the mechanism by which it exerts any function effect.

Many of the techniques and approaches applied to structure-based drug design described above rely at some stage on X-ray analysis to identify the binding position of a binding partner in a ligand-protein complex. A common way of doing this is to perform X-ray crystallography on the complex, produce a difference Fourier electron density map, and associate a particular pattern of electron density with the binding partner. However, in order to produce the map (as explained e.g. by Blundell et al., in Protein Crystallography, Academic Press, New York, London and San Francisco, (1976)), it is necessary to know beforehand the protein three dimensional structure (or at least a set of structure factors for the protein crystal). Therefore, determination of the turkey β1-AR structure also allows difference Fourier electron density maps of β1-AR-binding partner complexes to be produced, determination of the binding position of the binding partner and hence may greatly assist the process of rational drug design.

Accordingly, a sixth aspect of the invention provides a method for predicting the three dimensional structure of a binding partner of unknown structure, or part thereof, which binds to β1-AR, comprising: providing the coordinates of the turkey β1-AR structure of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof; providing an X-ray diffraction pattern of β1-AR complexed with the binding partner; and using the coordinates to predict at least part of the structure coordinates of the binding partner.

In one embodiment, the X-ray diffraction pattern is obtained from a crystal formed by soaking a crystal of β1-AR with the binding partner to form a complex. Alternatively, the X-ray diffraction pattern is obtained from a crystal formed by cocrystallising the β1-AR with the binding partner as described above. Alternatively, protein crystals containing a first binding partner can be back-soaked to remove this binding partner and the resultant crystals transferred into a second solution containing a second binding partner as described above.

A mixture of compounds may be soaked or co-crystallized with a turkey β1-AR crystal, wherein only one or some of the compounds may be expected to bind to the turkey β1-AR. The mixture of compounds may comprise a ligand known to bind to turkey β1-AR. As well as the structure of the complex, the identity of the complexing compound(s) is/are then determined.

Preferably, the methods of the previous aspects of the invention are computer-based. For example, typically the methods of the previous aspects of the invention make use of the computer systems and computer-readable storage mediums of the ninth and tenth aspects of the invention.

A seventh aspect of the invention provides a method for producing a binding partner of β1-AR comprising: identifying a binding partner according to the third, fourth, fifth or sixth aspects of the invention and synthesising the binding partner.

The binding partner may be synthesised using any suitable technique known in the art including, for example, the techniques of synthetic chemistry, organic chemistry and molecular biology.

It will be appreciated that it may be desirable to test the binding partner in an in vivo or in vitro biological system in order to determine its binding and/or activity and/or its effectiveness. For example, its binding to a β1-AR may be assessed using any suitable binding assay known in the art including the examples described above.

Moreover, its effect on β1-AR function in an in vivo or in vitro assay may be tested. For example, the effect of the binding partner on the β1-AR signalling pathway may be determined. For example, the activity may be measured by using a reporter gene to measure the activity of the β1-AR signalling pathway. By a reporter gene we include genes which encode a reporter protein whose activity may easily be assayed, for example β-galactosidase, chloramphenicol acetyl transferase (CAT) gene, luciferase or Green Fluorescent Protein (see, for example, Tan et al, 1996 EMBO J. 15(17): 4629-42). Several techniques are available in the art to detect and measure, expression of a reporter gene which would be suitable for use in, the present invention. Many of these are available in kits both for determining expression in vitro and in vivo. Alternatively, signalling may be assayed by the analysis of downstream targets. For example, a particular protein whose expression is known to be under the control of a specific signalling pathway may be quantified. Protein levels in biological samples can be determined using any suitable method known in the art. For example, protein concentration can be studied by a range of antibody based methods including immunoassays, such as ELISAs, western blotting and radioimmunoassays

An eight aspect of the invention provides a binding partner produced by the method of the seventh aspect of the invention.

Following identification of a binding partner, it may be manufactured and/or used in the preparation, i.e. manufacture or formulation, of a composition such as a medicament, pharmaceutical composition or drug. These may be administered to individuals.

Accordingly, the invention includes a method for producing a medicament, pharmaceutical composition or drug, the process comprising: (a) providing a binding partner according to the eighth aspect of the invention and (b) preparing a medicament, pharmaceutical composition or drug containing the binding partner.

The medicaments may be used to treat hypertension and cardiovascular disease (including congestive heart failure) and cardiovascular disease in the context of metabolic disease (eg diabetes and/or obesity) and/or respiratory disease (eg COPD (chronic obstructive pulmonary disease)).

The invention also provides systems, particularly a computer system, intended to generate structures and/or perform optimisation of binding partner which interact with β1-AR, β1-AR homologues or analogues, complexes of β1-AR with binding partners, or complexes of β1-AR homologues or analogues with binding partners.

Accordingly, a ninth aspect of the invention provides a computer system, intended to generate three dimensional structural representations of β1-AR, β1-AR homologues or analogues, complexes of β1-AR with binding partners, or complexes of β1-AR homologues or analogues with binding partners, or, to analyse or optimise binding of binding partners to said β1-AR or homologues or analogues, or complexes thereof, the system containing computer-readable data comprising one or more of:

-   -   (a) the coordinates of the turkey β1-AR structure of Table A,         Table B, Table C or Table D, optionally varied by a root mean         square deviation of residue backbone atoms of not more than         1.235 Å, or selected coordinates thereof;     -   (b) the coordinates of a target β1-AR homologue or analogue         generated by homology modelling of the target based on the data         in (a);     -   (c) the coordinates of a binding partner generated by         interpreting X-ray crystallographic data or NMR data by         reference to the coordinates of the turkey β1-AR structure, of         Table A, Table B, Table C or Table D, optionally varied by a         root mean square deviation of residue backbone atoms of not more         than 1.235 Å, or selected coordinates thereof, and     -   (d) structure factor data derivable from the coordinates of         (a), (b) or (c).

For example the computer system may comprise: (i) a computer-readable data storage medium comprising data storage material encoded with the computer-readable data; (ii) a working memory for storing instructions for processing said computer-readable data; and (iii) a central-processing unit coupled to said working memory and to said computer-readable data storage medium for processing said computer-readable data and thereby generating structures and/or performing rational drug design. The computer system may further comprise a display coupled to the central-processing unit for displaying structural representations.

The invention also provides such systems containing atomic coordinate data of target proteins of unknown structure wherein such data has been generated according to the methods of the invention described herein based on the starting data provided in Table A, Table B, Table C or Table D optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof.

Such data is useful for a number of purposes, including the generation of structures to analyse the mechanisms of action of binding partners and/or to perform rational drug design of binding partners which interact with β1-ARs, such as compounds which are agonists or antagonists.

A tenth aspect of the invention provides a computer-readable storage medium, comprising a data storage material encoded with computer readable data, wherein the data comprises one or more of:

-   -   (a) the coordinates of the turkey β1-AR structure of Table A,         Table B, Table C or Table D, optionally varied by a root mean         square deviation of residue backbone atoms of not more than         1.235 Å, or selected coordinates thereof;     -   (b) the coordinates of a target β1-AR homologue or analogue         generated by homology modelling of the target based on the data         in (a);     -   (c) the coordinates of a binding partner generated by         interpreting X-ray crystallographic data or NMR data by         reference to the coordinates of the turkey β1-AR structure of         Table A, Table B, Table C or Table D, optionally varied by a         root mean square deviation of residue backbone atoms of not more         than 1.235 Å, or selected coordinates thereof, and     -   (d) structure factor data derivable from the coordinates of         (a), (b) or (C).

The invention also includes a computer-readable storage medium comprising a data storage material encoded with a first set of computer-readable data comprising a Fourier transform of at least a portion of the structural coordinates of turkey β1-AR, of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof; which data, when combined with a second set of machine readable data comprising an X-ray diffraction pattern of a molecule or molecular complex of unknown structure e.g. a target protein of unknown structure, using a machine programmed with the instructions for using said first set of data and said second set of data, can determine at least a portion of the structure coordinates corresponding to the second set of machine readable data.

The invention also provides a computer-readable data storage medium comprising a data storage material encoded with a first set of computer-readable data comprising the structural coordinates of turkey β1-AR, of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof; which, when combined with a second set of machine readable data comprising an X-ray diffraction pattern of a molecule or molecular complex of unknown structure, e.g. a target protein of unknown structure, using a machine programmed with the instructions for using said first set of data and said second set of data, can determine at least a portion of the electron density corresponding to the second set of machine readable data.

It will be appreciated the that the computer-readable storage media of the invention may comprise a data storage material encoded with any of the data generated by carrying out any of the methods of the invention relating to structure solution and selection/design of binding partners to β1-AR and drug design.

The invention also includes a method of preparing the computer-readable storage media of the invention comprising encoding a data storage material with the computer-readable-data.

As used herein, “computer readable media” refers to any medium or media, which can be read and accessed directly by a computer. Such media include, but are not limited to: magnetic storage media such as floppy discs, hard disc storage medium and magnetic tape; optical storage media such as optical discs or CD-ROM; electrical storage media such as RAM and ROM; and hybrids of these categories such as magnetic/optical storage media.

By providing such computer readable media, the atomic coordinate data of the invention can be routinely accessed to model β1-AR or selected coordinates thereof.

For example, RASMOL (Sayle et al., TIBS, Vol. 20, (1995), 374) is a publicly available computer software package, which allows access and analysis of atomic coordinate data for structure determination and/or rational drug design.

As used herein, “a computer system” refers to the hardware means, software means and data storage means used to analyse the atomic coordinate data of the invention. The minimum hardware means of the computer-based systems of the present invention comprises a central processing unit (CPU), input means, output means and data storage means. Desirably a monitor is provided to visualize structure data. The data storage means may be RAM or means for accessing computer readable media of the invention. Examples of such systems are microcomputer workstations available from Silicon Graphics Incorporated and Sun Microsystems running Unix based, Windows XP or IBM OS/2 operating systems.

An eleventh aspect of the invention provides a method for providing data for generating three dimensional structural representations of β1-AR, β1-AR homologues or analogues, complexes of β1-AR with binding partners, or complexes of β1-AR homologues or analogues with binding partners, or, for analysing or optimising binding of binding partners to said β1-AR or homologues or analogues, or complexes thereof, the method comprising:

-   -   (i) establishing communication with a remote device containing         computer-readable data comprising at least one of:         -   (a) the coordinates of the turkey β1-AR structure of Table             A, Table B, Table C or Table D, optionally varied by a root             mean square deviation of residue backbone atoms of not more             than 1.235 Å, or selected coordinates thereof;         -   (b) the coordinates of a target β1-AR homologue or analogue             generated by homology modelling of the target based on the             data in (a);         -   (c) the coordinates of a binding partner generated by             interpreting X-ray crystallographic data or NMR data by             reference to the coordinates of the turkey β1-AR structure             of Table A, Table B, Table C or Table D, optionally varied             by a root mean square deviation of residue backbone atoms of             not more than 1.235 Å, or selected coordinates thereof, and         -   (d) structure factor data derivable from the coordinates of             (a), (b) or (c); and     -   (ii) receiving said computer-readable data from said remote         device.

The computer-readable data received from said remote device, particularly when in the form of the coordinates of the turkey β1-AR structure of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof, may be used in the methods of the invention described herein, e.g. for the analysis of a binding partner structure with a β1-AR structure.

Thus the remote device may comprise e.g. a computer system or computer readable media of one of the previous aspects of the invention. The device may be in a different country or jurisdiction from where the computer-readable data is received.

The communication may be via the internet, intranet, e-mail etc, transmitted through wires or by wireless means such as by terrestrial radio or by satellite. Typically the communication will be electronic in nature, but some or all of the communication pathway may be optical, for example, over optical fibers.

A twelfth aspect of the invention provides a method of obtaining a three dimensional structural representation of a crystal of a turkey β1-AR, which method comprises providing the coordinates of the turkey β1-AR structure of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof, and generating a three-dimensional structural representation of said coordinates.

For example, the structural representation may be a physical representation or a computer generated representation. Examples of representations are described above and include, for example, any of a wire-frame model, a chicken-wire model, a ball-and-stick model, a space-filling model, a stick model, a ribbon model, a snake model, an arrow and cylinder model, an electron density map or a molecular surface model.

Computer representations can be generated or displayed by commercially available software programs including for example QUANTA (Accelrys .COPYRIGHT. 2001, 2002), O (Jones et al., Acta Crystallogr. A47, pp. 110-119 (1991)) and RIBBONS (Carson, J. Appl. Crystallogr., 24, pp. 9589-961 (1991)).

Typically, the computer used to generate the representation comprises (i) a computer-readable data storage medium comprising a data storage material encoded with computer-readable data, wherein said data comprise the coordinates of the turkey β1-AR structure; of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof; and (ii) instructions for processing the computer-readable data into a three-dimensional structural representation. The computer may further comprise a display for displaying said three-dimensional representation.

A thirteenth aspect of the invention provides a method of predicting one or more sites of interaction of a β1-AR or a homologue thereof, the method comprising: providing the coordinates of the turkey β1-AR structure of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof; and analysing said coordinates to predict one or more sites of interaction.

For example, a binding region of a β1-AR for a particular binding partner can be predicted by modelling where the structure of the binding partner is known. Typically, the fitting and docking methods described above would be used. This method may be used, for example, to predict the site of interaction of a G protein of known structure as described in viz Gray J J (2006) Curr Op Struc Biol Vol 16, pp 183-193.

A fourteenth aspect of the invention provides a method for assessing the activation state of a structure for β1-AR, comprising: providing the coordinates of the turkey β1-AR structure, of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof; performing a statistical and/or topological analysis of the coordinates; and comparing the results of the analysis with the results of an analysis of coordinates of proteins of known activation states.

For example, protein structures may be compared for similarity by statistical and/or topological analyses (suitable analyses are known in the art and include, for example those described in Grindley et al (1993) J Mol Biol Vol 229: 707-721 and Holm & Sander (1997) Nucl Acids Res Vol 25: 231-234). Highly similar scores would indicate a shared conformational and therefore functional state eg the inactive antagonist state in this case.

One example of statistical analysis is multivariate analysis which is well known in the art and can be done using techniques including principal components analysis, hierarchical cluster analysis, genetic algorithms and neural networks.

By performing a multivariate analysis of the coordinate data of the turkey β1-AR structure of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å or selected coordinates thereof, and comparing the result of the analysis with the results of the analysis performed on coordinates of proteins with known activation states, it is possible to determine the activation state of the coordinate set analysed. For example, the activation state may be classified as ‘active’ or ‘inactive’.

A fifteenth aspect of the invention provides a method of producing a protein with a binding region that has substrate specificity substantially identical to that of β1-AR, the method comprising

-   -   a) aligning the amino acid sequence of a target protein with the         amino acid sequence of a β1-AR;     -   b) identifying the amino acid residues in the target protein         that correspond to any one or more of the following positions         according to the numbering of the turkey β1-AR as set out in         FIG. 6: 117, 118, 121, 122, 125, 201, 203, 207, 211, 215, 306,         307, 310 and 329; and     -   c) making one or more mutations in the amino acid sequence of         the target protein to replace one or more identified amino acid         residues with the corresponding residue in the turkey β1-AR.

By “an amino acid residue that corresponds to” we include an amino acid residue that aligns to the given amino acid residue in turkey β1-AR when the turkey β1-AR and target protein are aligned using e.g. MacVector and CLUSTALW.

For example, amino acid residues contributing to the ligand binding site of β1-AR include amino acid residues 117, 118, 121, 122, 125, 201, 203, 207, 211, 215, 306, 307, 310 and 329. Thus a binding site of a particular protein may be engineered using well known molecular biology techniques to contain any one or more of these residues to give it the same substrate specificity. This technique is well known in the art and is described in, for example, Ikuta et al (J Biol Chem (2001) 276, 27548-27554) where the authors modified the active site of cdk2, for which they could obtain structural data, to resemble that of cdk4, for which no X-ray structure was available.

Preferably, all 14 amino acids in the target portion which correspond to amino acid residues 117, 118, 121, 122, 125, 201, 203, 207, 211, 215, 306, 307, 310 and 329 of the turkey β1-AR are, if different, replaced. However, it will be appreciated that only 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, 2 or 1 amino acid residues may be replaced.

Preferences for the target protein are as defined above with respect to the first aspect of the invention.

A sixteenth aspect of the invention provides a method of predicting the location of internal and/or external parts of the structure of β1-AR or a homologue thereof, the method comprising: providing the coordinates of the turkey β1-AR structure of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof and analysing said coordinates to predict the location of internal and/or external parts of the structure.

For example, from the three dimensional representation, it is possible to read off external parts of the structure, eg surface residues, as well as internal parts, eg residues within the protein core. It will be appreciated that the identification of external protein sequences will be especially useful in the generation of antibodies against a β1-AR.

A seventeenth aspect of the invention provides a peptide of not more than 100 amino acid residues in length comprising at least five contiguous amino acid residues which define an external structural moiety of the β1-AR.

Examples of suitable external structural moieties include the six surface loops of contiguous residues and the three surface (non-transmembrane) helices as follows:

-   -   CL1 Residues 68-76     -   EL1 Residues 99-116     -   CL2 (short surface helix) Residues 143-145     -   EL2 (short surface helix) Residues 174-207     -   EL3 Residues 311-319     -   H8 (short surface helix) Residues 341-358

Thus in one embodiment, the peptide of not more than 100 amino acid residues comprises at least five contiguous amino acid residues from any of the external structural moieties defined above. It will be appreciated that the peptide may comprise at least five contiguous amino acid residues from one external structural moiety defined above and five contiguous amino acid residues from one or more different external structural moieties defined above.

It will be appreciated that such peptides may serve as epitopes for the generation of binding partners, e.g. antibodies against a β1-AR. Thus, the invention also includes a binding partner selected to bind to the peptide of the eighteenth aspect of the invention.

The crystallisation of the turkey β1-AR has led to many interesting observations about its structure, including its ligand binding site. Thus it will be appreciated that the invention allows for the generation of mutant β1-ARs wherein residues corresponding to these areas of interest are mutated to determine their effect on β1-AR function and ligand binding specificity.

Accordingly, an eighteenth aspect of the invention provides a mutant β1-AR, wherein the β1-AR before mutation has a binding region in the position equivalent to the binding region of turkey β1-AR that is defined by residues including 117, 118, 121, 122, 125, 201, 203, 207, 211, 215, 306, 307, 310 and 329 of β1-AR according to the numbering of the turkey β1-AR as set out in FIG. 6 and wherein one or more residues equivalent to 117, 118, 121, 122, 125, 201, 203, 207, 211, 215, 306, 307, 310 and 329 forming part of the binding region of β1-AR is mutated.

Residues in proteins can be mutated using standard molecular biology techniques as are well known in the art.

A nineteenth aspect of the invention provides a method of making a β1-AR crystal comprising: providing purified β1-AR; and crystallising the β1-AR either by using the sitting drop or hanging drop vapour diffusion technique, using a precipitant solution comprising 0.1M ADA (N-(2-acetamido) iminodiacetic acid) (pH5.6-9.5). and 25-35% PEG 600.

In a preferred embodiment, the precipitant solution comprises 0.1M ADA (pH 6.9-7.3) and 29-32% PEG600. However, it will be appreciated that any other buffer at a concentration between 0.03 and 0.30 M may be used, and that any PEG from PEG400 to PEG5000 may be used.

A twentieth aspect of the invention provides a crystal of β1-AR having the structure defined by the coordinates of the turkey β1-AR structure of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof. Typically, the crystal has a resolution of 2.7 Å or better.

The space group of the crystal may be either P1 or C2.

Thus, in one embodiment the crystal has P1 symmetry with unit cell dimensions a=55.5 Å±1 Å, b=86.8 Å±, 20 Å, c=95.50 Å±20 Å.

In another embodiment, the crystal has C2 symmetry with unit cell dimensions a=145-195 Å±20 Å, b=55.5 Å±1 Å, c=85-120 Å.

The invention also includes a co-crystal of β1-AR having the structure defined by the coordinates of the turkey β1-AR structure of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof, and a binding partner. Typically, the crystal has a resolution of 2.7 Å or better.

The invention includes the use of the coordinates of the turkey β1-AR structure of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof to solve the structure of target proteins of unknown structure.

The invention includes the use of the coordinates of the turkey β1-AR structure of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof to identify binding partners of a β1-AR.

The invention includes the use of the coordinates of the turkey β1-AR structure of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof in methods of drug design where the drugs are aimed at modifying the activity of the β1-AR.

The invention will now be described in more detail with respect to the following Figures and Examples wherein:

FIG. 1 (A) Schematic diagram of the β1 sequence in relation to secondary structure elements. Amino sequence in white circles indicates regions that are well ordered, but sequences in a grey circle were not resolved in the structure. Grey sequences on an orange background were deleted to make the β1 construct for expression. Thermostabilising mutations are in red and two other mutations C116L and C358A are in blue. The Na⁺ is in purple and the two disulphide bonds are depicted as dotted lines. Numbers refer to the first amino acid residue in each helix, with the Ballesteros-Weinstein numbering in superscript. (B) Ribbon representation of the β1 structure. The N-terminus, C-terminus, the Na⁺ ion, the two disulphide bonds extracellular loop 2 (EL2) and intracellular loops 1 and 2 (CL1, CL2) are labelled (C) B factors depicted on a ribbon representation of the β1 configuration. Order of B factors from low to high is EW, H4, H3, H7, H5, H2, H6, EL2, CL2, H1, EL3, CL3, CL1, N-term and H8C-term.

FIG. 2 (A) Packing of the β1 molecules in the C2 and P1 crystals obtained, showing how the packing is related. (B) Ribbon representation of the molecules within one unit cell of the P1 crystal form. Octylthiomaltoside detergent molecules, which pack at the interfaces between the receptors, are shown in pink.

FIG. 3 Representative regions of electron density in the structure. (A) Co-ordination of the Na⁺ by the backbone carbonyl groups from amino acid residues Cys192, Asp195, Cys198 and a water molecule. (B) Water molecule hydrogen bonded to Trp303 in helix 6.

FIG. 4 The ligand binding region. (A) 2Fo-Fc omit map showing the unrefined density for cyanopindolol after molecular replacement using only the peptide co-ordinates form human β2 receptor. (B) and (C) Position of amino acid residues that interact with the ligand cyanopindolol.

FIG. 5 (A) Comparison of the CL2 loop region between the b1 structure (yellow), the β2-T4 lysozyme fusion (green), the β2-Fab complex (mauve) and rhodopsin (purple). (B) Comparison of the ionic regions in β1, rhodopsin and the two β2 structures. The amino acid residues shown in the β1 structure are Tyr149^(3.60), Asp138^(3.49), Arg139^(3.50) and Glu285^(6.29).

FIG. 6 Alignment of the turkey β-adrenergic receptor with human β1, β2 and β3 receptors.

FIG. 7 Multiple sequence alignment of turkey β1-AR (beta 36/m23 construct) with (1) β2-AR T4 lysozyme fusion protein (structure of which is described in Cherezov et al (2007) and Rosenbaum et al (2007)) and (2) β2-AR (β2-AR 365 construct, structure of which is described in Rasmussen et al (2007)).

FIG. 8 Distances between corresponding Cα atoms after superposition of β1-AR-m23 and the human β2-AR (PDB no: 2RH1) compared with superposition of molecules A and B of β1-AR-m23.

FIG. 9 (A) Size exclusion elution profiles of Beta 6 and Beta 36 (B) SDS PAGE of Beta 6 and Beta 36

FIG. 10 Size-exclusion profiles of Beta 36 in dodecylmaltoside (left peak, eluted earlier), and Beta 36/m23 in nonylglucoside (right peak, eluted later).

FIG. 11 Activation of G-proteins by m23 mutant receptor as measured by ATP binding as a function of adrenaline concentration and its inhibition by antagonist propranolol. This demonstrates that the inverse agonist ICI118551 does not depress the cAMP accumulation. Both panels show the pharmacological behaviour of m23.

FIG. 12 Relationship between cyanopindolol in beta1 and carazolol in beta2 and the residues Phe325 in beta1 and Tyr308 in beta2, together with one possible interaction which might occur between hydroxyl groups of ceratin sub-type specific ligands and the hydroxyl group of Tyr308 in beta2.

EXAMPLE 1 Structure Determination of Turkey β1-AR Introduction

The G protein coupled receptor superfamily has a major role in transmembrane signal transduction in organisms from yeast to man and many are important biomedical drug targets. We report the 2.7 Å resolution crystal structure of a β1 adrenergic receptor (b1AR), whose conformation and improved thermostability have been selected by systematic mutagenesis and binding to the antagonist, cyanopindolol. The receptor mutant, b1AR-m23, is in an inactive conformation and there is no ionic lock present between helix 3 and 7. The interactions of cyanopindolol with the β1 receptor are similar to those of carazolol with β2AR, though some small significant differences help to understand important aspects of the selectivity between β1 and β2 antagonists. There is a well-defined helix in cytoplasmic loop 2, absent in the b2 structures, which directly links this region to which G proteins bind upon agonist binding to the highly conserved DRY motif at the end of helix 3 essential for receptor activation.

Results and Discussion Crystallisation of the β1 Adrenergic Receptor

There are two major prerequisites to the crystallisation of any membrane protein, once the problems of overexpression and purification have been overcome. Firstly, the protein must be sufficiently stable in detergent solution for crystals to form and, secondly, the protein must exist primarily in a single conformational state. GPCR crystallisation is therefore extremely challenging, because they are usually unstable in detergent and spontaneously cycle between an inactive antagonised state (R) and an active agonist-bound state (R*), even in the absence of ligands. Both recent structures of β2 required the receptor to be bound to the partial inverse agonist carazolol, so that the receptors were all in a single antagonised (R) conformation. The human β2 receptor was sufficiently stable to purify in mild detergents such as DDM, but crystals were only obtained either when β2 was bound to a specific F_(ab) fragment from a conformationally neutral monoclonal antibody (Day et al (2007) Nat Methods 4(11): 927-9) or by the selection of a protease-resistant T4 lysozyme fusion (Rosenbaum et al., 2007); in both cases the additional proteins made essential lattice contacts within the crystals, and in the T4 fusion induced constitutive activation. Stabilisation of the receptor during crystallisation was either achieved by the formation of detergent-lipid bicelles (DMPC/CHAPSO) around the protein (Rasmussen et al, 2007) or by the use of cholesterol-doped lipidic cubic phases (Cherezov et al, 2007).

The human β1 receptor has proven more difficult to purify than β2, because it is unstable once solubilised in detergent, so we therefore used the turkey β1 receptor which is considerably more stable than its human homologue (Parker & Ross). Short-chain detergents, such as nonyl- and octyl-glucosides, are the best choice for crystallisation of small membrane proteins, but β1 was unstable in them and precipitated upon detergent exchange (Warne et al 2003). We therefore expressed β1 in an Escherichia coli expression system (Grisshammer et al) and evolved it into a conformationally thermostabilised form (β1-m23) that is stable even in short-chain detergents (Serrano PNAS). The six point mutations in β1-m23 not only increased the thermostability of the receptor in dodecylmaltoside (DDM) by 21° C., but also altered the equilibrium between R and R* so that the mutant receptor was preferentially in the antagonised (R) state (Serrano-Vega et al 2008). The receptor construct that crystallised (FIG. 1) has deletions at the N-terminus, C-terminus and in cytoplasmic loop 3 to remove regions that were predicted to be unstructured (Warne et al 2003). It also contains 8 point mutations, 6 for thermostabilisation (R68^(1.59)S, M90^(2.52)V, Y227^(5.58)A, A282^(6.27)L, F327^(7.38)A, F338^(7.49)M), one for improved expression (C116^(3.27)L) and one for the removal of a palmitoylation site (C358^(8.53)A).

Pharmacological Analysis of β1-m23

In any crystallographic study it is essential to define exactly what conformational state the receptor is in to understand how function relates to structure. In a pharmacological analysis, the mutant receptor β1-m23 bound the antagonists dihydroalprenolol and cyanopindolol with similar affinities to the wild-type receptor, but the agonists noradrenaline and isoprenaline bound more weakly by a factor of 2470 and 650 respectively (Serrano-Vega et a/). This reflects a change in the preferentially adopted global conformation of the receptor to an antagonised state. The structure we have determined contains cyanopindolol in the binding region; it is known that cyanopindolol binds to β1-m23 with very high affinity (60 pM) and that it is an antagonist. Thus the structure determined is that of β1 in the antagonised (inverse agonist) conformation.

Overall Structure of the β1 Receptor

Crystals of β1-m23 were obtained in octylthioglucoside after an extensive crystallisation screen. Two closely related crystal forms with either C2 or P1 symmetry were observed; the packing is very similar in both space groups, with 4 molecules in the P1 unit cell and 8 in the C2 cell, which has one axis twice as large as the comparable axis in the P1 cell. The pairs of molecules related by noncrystallographic symmetry in C2 are slightly rotated to give the P1 form (FIG. 2) The C2 crystals diffracted anisotropically with diffraction limits varying between 2.6-3.5 Å, whereas the P1 crystals showed isotropic diffraction to beyond 2.7 Å. The β1 structure was solved to 2.7 Å (Table 1) by molecular replacement. The four receptor molecules (A-D) were independently refined, and thus allow four different views of the same molecule. Molecules B and C are similar to each other (rmsd 0.18 Å for 273 residues) and molecules A and D are also similar to each other (rmsd 0.22 Å for 273 residues); molecules A and D both differ from molecules B and C by an average rmsd of 0.48 Å. The major difference between molecules A & D and B & C (which was excluded from the above comparison) is that there is outward kink of the 12 N-terminal residues of helix 1 (Trp40-Val51) by about 60°, which accommodates molecules A & D within the crystal lattice: the helix boundaries and overall structural motifs are presented in FIG. 1. There is well-defined density for all the transmembrane helices, extracellular loops (1-3), two intracellular loops (CL1 & 2) and helix 8 (except in molecule C). There was no density corresponding to most of CL3 due to disorder. Included in the structure are well-ordered detergent molecules of octylthioglucoside that sometimes make essential contacts between neighbouring receptor molecules. In addition, there is one Na⁺ ion per receptor and 5-9 well-defined water molecules (FIG. 3) per receptor. Unless otherwise stated, all further discussion refers to molecule B, as only this molecule has an unkinked helix 1 and includes helix 8.

The amino acid sequence of the turkey β1 receptor is 65% identical to that of the human β2 receptor over residues 39-358 excluding CL3 residues 238-285 i.e. excluding the N- and C-termini and CL3) and it is therefore unsurprising that the structure of the transmembrane regions of β1 and β2 are very similar. The best superposition of the β2 (2rh1) and β1 (chain B) structure is based on selected residues in helices 3,5,6,7, as these helices form most of the ligand binding region; 78 alpha carbons can be superimposed with an rmsd of 0.25 Å. The rmsd over all the transmembrane helices is 0.4 Å for backbone (C-α, C, N atoms). In addition, the structure of the three extracellular loops in β1AR are very similar to β2AR with an overall rms deviation of 0.83 Å for backbone atoms (C-α, C, N in extracellular loops), which is consistent with high sequence conservation of these regions in the DAR family (FIG. 6). On the extracellular surface, there is a sodium ion co-ordinated by the carbonyl groups in the peptide backbone from residues Cys192, Asp195, Cys198 and one water molecule. The sodium ion was assigned based upon its coordination geometry and its presence at the negative end of the EL2 α-helix dipole is in a position often favoured by positive ions or ligands.

Overall, 27 water molecules were built into the map (Table 2) using the criteria that spherical densities must be >1.0σ in the 2Fo-Fc difference map and they must form at least two H-bonds with good geometry. Only one water molecule was likely to be important structurally as it maintains the structure of the kink in helix 6 and H-bonds to W303, which is thought to be important in the light-activation of rhodopsin. All other waters tended to be less buried, and none are absolutely conserved between β1 and β2, or even between the different molecules of β1 in the same unit cell. Other water molecules must be present throughout the core of the β1 structure to, solvate polar amino acid residues, but they must be only partially ordered and are therefore unlikely to have a strong influence on substrate specificity, although they could affect the overall stability of each state of the receptor, as well as the equilibrium between R and R*.

The 6 point mutations that thermostabilised β1 were essential for obtaining well-diffracting crystals (Serrano-Vega et al 2008). It is not clear, now the structure has been solved, why the mutations make β1AR-m23 more thermostable than the wild type β1 receptor. At each mutated position there were no significant changes in the Cα backbone when compared with the 62 structure and, therefore, the mutations have not distorted the structure of the receptor. This is consistent with the observations that β1AR-m23 binds antagonists with similar affinities to the wild type receptor (Serranno-Vega et al 2008) and that it can couple efficiently to G. proteins.

Structure of the Cytoplasmic Loops

All three βAR structures have a similar conformation of CL1, but there are major differences in CL3; these differences are not of physiological relevance because they arise due to either partial deletion of the loop (β1), partial deletion and insertion of T4 lysozyme (β2-T4) or by formation of a complex with an antibody fragment (β2:Fab). However, differences in the structure of CL2 (FIG. 5) are important, because this region is highly conserved and the amino acid sequence is unchanged in each of the three βARs crystallised. In β1, CL2 forms a short α-helix whereas in both the β2 structures and in rhodopsin this region is in an extended conformation (FIG. 5). In the β2:Fab structure the second intracellular loop is in contact with the neighboring antibody fragment (Rassmusen et al 2007) and might therefore be displaced. In the human β2-T4 structure an α-helix in CL2 may not be present because of lattice contacts involving the lysozyme fusion protein and the N-terminus of CL2 (Cherezov et al, 2007).

The CL2 loop has been proposed to function as the switch enabling G protein activation (Burstein et al 1998) and, from the β1 structure, it is clear that this region also has an important contact to the adjacent highly conserved D^(3.49)R^(3.50)Y^(3.51) motif in helix 3. In rhodopsin, there is a salt bridge formed between Arg^(3.50) and Glu^(6.30), the ionic lock, which has been proposed to play an essential role in maintaining all GPCRs in an inactive state (Ballesteros et al (2001) JBC 276, 29171-29177) but is subsequently broken upon receptor activation. In none of the adrenergic receptor structures is there an ionic interaction between the Arg139^(3.50) of the DRY motif and the Glu285^(8.30) in helix 6; as the structure of β1 is of the antagonised state, there is, therefore, no interhelical ionic lock in the inactive state of this receptor and, by implication, all βARs (FIG. 5). This is mainly due to the increased distance between the C_(α) atoms of Arg^(3.50) and Glu^(6.30) in β1 (10.9 Å) and β2 (11.2 Å) compared with rhodopsin (8.7 Å). There is, however, an intrahelical interaction between Asp^(3.49) and Arg^(3.59) of the DRY motif in all three β3AR structures. The helical conformation of CL2 in the β1 structure positions Tyr149^(3.89) sufficiently close to Asp138^(3.49) of the DRY motif to allow the formation of a H-bond. Supporting evidence for this structural role of Tyr149^(3.89) comes from the observation that the Y149A mutation makes β1AR much less thermally stable (Table 3). The equivalent Tyr141^(3.60) in both β2 structures is in a cavity between helix 3, 4 and 6, but the biological relevance of this is unclear, due to the perturbations in this region caused by either the T4 lysozyme fusion or by the bound antibody F_(ab). Interestingly, CL2 was predicted to be α-helical based upon a mutagenic study of the m5 muscarinic receptor and the mutation Y138^(3.80)A led to increased constitutive activity in the receptor (Burstein at al 1998).

The Ligand Binding Region and the Selectivity of β Receptor Antagonists

The β1AR was crystallised in the presence of cyanopindolol, which is similar in structure to carazolol that is present in the ligand binding region of both β2 structures; both these ligands bind with very high affinity to all β1-ARs and β2-ARs. In the β1 structure there are 14 amino acid residues whose side chains make contacts with cyanopindolol in the ligand binding region; 5 side chains are from helix 3, 3 each from helices 5 and 6, one from helix 7 and 2 from EL2. All these residues are identical to those in β2 and the mode of binding of cyanopindolol to β1 is, therefore, very similar to that of carazolol in β2. However, the extra benzene ring in carazolol, due to a van der Waals contact with Y199^(5.38), pushes the ligand more deeply into the binding site, by 0.8 Å. The nitrogen in the cyano-moiety of cyanopindolol makes a hydrogen bond with the hydroxyl of T203^((5.34)) which is located together with F201^(5.32) at the inner most strand of EL2 that comes close to the ligand (FIG. 4). The same H-bonds between the ligand and D121^((3.32)), N329^((7.39)) and S211^((5.42)) are present in both complexes, but the rotamer conformation of S211 is different.

Cyanopindolol and carazolol are non-specific RAR ligands, so it is unsurprising that they bind to β1 and β2 similarly. To explain why some ligands preferentially bind to either β1 or β2, there must be consistent differences in amino acid residues close to the ligand binding region to have either a direct or indirect effect on ligand binding; at the opposite extreme, there must be global changes in the binding site due to multiple differences throughout the protein domain, as illustrated in FIG. 8. Regarding the former mechanism, a comparison of residues within 8 Å of the binding region amongst all β2 and β1 receptors identified only two residues that are highly conserved but different between the two receptor families. The respective residues are Val172 and Phe325 in β1, which are equivalent to Thr164 and Tyr308 in β2; both these changes introduce polar residues into the binding region of β2 relative to β1 and, therefore, could have a profound effect upon ligand binding and selectivity, either directly or via a different distribution of water molecules. Tyr308 has also been implied by a mutagenesis study to be important for the agonist selectivity by mutagenesis (Kikkawa et al (1998) Mol Pharmacol 53: 128-134). The closest distance between cyanopindolol and the side chain of Vail 72 or Phe325 is 8 Å or 6 Å respectively. In the β2 receptor, Tyr308 is maintained closer to the binding region via a hydrogen bond to Asn293 and it is close to the carazolol heterocyclic ring, but in the β1 receptor the equivalent residue, Phe325, moves away from the binding region and the Asn310 side chain changes position to make a hydrogen bond with the cyano group of cyanopindolol; therefore there is no contact between Phe325 in β1 and cyanopindolol. The presence of Tyr308 adjacent to the carazolol heterocyclic ring and the absence of an equivalent H-bond acceptor in β1 suggests that one mechanism for the specificity differences β1 and β2 antagonists could be the presence of a H-bond donor group at the end of the heterocycle. This is indeed the case for nadolol and timolol, which have similar extended chain structures to both carazolol and cyanopindolol at their aminergic ends, but differ in their heterocyclic regions (FIG. 12).

Another significant effector of ligand specificity and the kinetics of ligand binding is EL2; the Cα positions within this highly structured region differ from β2 by an rmsd of 1 Å. There are also significant differences in the amino acid sequences between β1 and β2 in the entrance to the ligand binding region. This changes the shape of the entrance to the ligand binding region with a bridge formed by a H-bond between Asp192 and Lys305 in β2 that is absent in β1 because the respective residues are Glu200^(5.31) and Val312^(6.57). Differences between β1 and β2 in this region could affect ligand selectivity in two ways. Firstly, some ligands have extensions that may make direct interactions with these sub-type specific residues. Secondly, the different physical characteristics of the entrance to the ligand binding region could affect the kinetics of ligand binding. Recent mutational studies not only show that EL2 defines the specificity, of allosteric modulators (Shi & Javitch 2004; Klco et al 2005; Scarselli et al 2007), but, in addition, the flexibility of the loop is important to the kinetics of modulator binding (Aviani et al 2007).

The structure of β1, when compared to β2, provides a sound basis for studying selectivity differences between RAR antagonists structurally similar to cyanopindolol and carazolol. However, many ligands, such as CGP 20712A and the agonist salmeterol, show very high selectivities (Baker 2005 BJP), but are structurally unrelated to either cyanopindolol or carazolol. These ligands could well bind to the βARs utilising additional amino acid residues to those described here. This is certainly the case for the binding of selective agonists such as for RO363 (Sugimoto at al, 2002) that cause a large conformational change upon binding; residues which are different between β1 and β2 and when mutated appear to be responsible for the differences in agonist affinity, are either distant from the cyanopindolol binding site on H2 facing the lipid phase (H β1AR L110^((2.66)) and T117^((2.63))) or form a second shell cap (H β1AR F359^((7.35))) on the binding region (Sugimoto et al, 2002). Thus further structures with a variety of ligands bound will be required to fully understand all the complexities of ligand selectivity in the βARs.

CONCLUSION

Two changes of consistently changed amino acids to more polar residues in beta 2 receptor close to the ligand site, and changes in the packing of amino acid side chains in the second shell of amino acid side chains which surrounds the antagonist ligand binding site modulate the detailed structure of the ligand binding site and must cause the observed differences in the pharmacological affinity profiles. These distant side chains are those which either make contact with the 14 side chains which do contact the ligand or are on the far side of the four transmembrane helices from which the 14 side chains protrude (H3, H5, H6, H7). Some of the more distant amino acid changes between β1AR and β2AR (also β3AR), of which there are over 100 highly subtype-conserved differences within the β-adrenergic family, must also contribute to the sub-type specificity. Thus the properties of the different members of the β-adrenergic GPCR subfamily in terms of pharmacology are due to the overall structure of the entire seven helix bundle with contributions from distant parts of the structure modulating the properties of the ligand binding site and its activation. Extrapolating to the related aminergic subfamilies and beyond, this implies that direct experimental observation of bound ligand structures will frequently be necessary and essential for successful design of selective drugs.

Methods Purification and Crystallisation

The β1 receptor construct T34-424/His6 for baculovirus expression that was described in Warne et al (2003) was used as the basis for the generation of the β36/m23 construct used to determine the structure reported here. The construct was further truncated at the C-terminus after Leu367, and 6 Histidines were added to allow purification by Ni²⁺-affinity chromatography (IMAC). Two segments, comprising residues 244-271 and 277-278 of the third intracellular loop were also deleted. The construct included the following 8 point mutations: C116L increased expression, C358A removed palmitoylation and helped crystallisation, R68S, M90V, Y227A, A282L, F327A and F338M thermostabilise the receptor. Baculovirus expression in High 5™ cells, membrane preparation, solubilization, IMAC and alprenolol sepharose chromatography were all as previously described (Warne et al 2003), except that solubilization and IMAC were performed in buffers containing the detergent decylmaltoside and the detergent was exchanged on the alprenolol sepharose column to octylthioglucoside; purified receptor was eluted from the alprenolol sepharose with cyanopindolol (30 μM). The buffer was exchanged to 10 mM Tris-HCl pH7.7, 50 mM NaCl, 0.1 mM EDTA, 0.35% octylthioglucoside and 0.5 mM cyanopindolol during concentration to give a final receptor concentration of 5.5-6.0 mg/ml.

With the thermally stabilised protein first a wide crystalisation screen was performed in 4 different detergents. A total of 58 mg of receptor was used to set up 17800 crystallisation trials in MRC UV transparent crystallisation sitting drop plates that were and imaged with the MRC multi wavelength imaging system at 380 nm. Promising looking crystals were then observed at 280 nm to exclude salt and detergent crystals. 280 nm absorbing crystals were picked and X-rayed using a 4 um beam at ID 13 ESRF. The receptor crystallisation was then optimised manually by vapour diffusion at 18° C. with either hanging or sitting drop methodology after addition of an equal volume of reservoir solution (0.1M N-(2-acetamido)iminodiacetic acid (ADA), pH 6.9-7.3 and 29-32% PEG 600). Crystals were mounted on Hampton CrystalCap HT™ loops and frozen in liquid nitrogen. The best cryoprotection of crystals was achieved by increasing the PEG 600 concentration in the drop to 55-70%.

Data Collection, Structure Solution and Refinement

The first diffraction patterns from microcrystals grown in the primary crystallisation screens were tested with a 5 μm beam at ID13 (Schertler & Riekel, 2005). The best crystallisation conditions were refined to improve diffraction quality and the optimised crystals were then screened at ID23-2 with a 10 μm focused beam; the micro-beams helped to deal with heterogeneous diffraction within a single crystal. Diffraction data were collected with a Mar 225 CCD detector on the microfocus beamline ID23-EH2 (λ=0.8726 Å) at the European Synchrotron Radiation Facility, Grenoble, using three positions on a single cryo-cooled crystal (100 K). The images were processed with MOSFLM (Leslie, Joint CCP4+ESF-EAMCB Newsletter on Protein Crystallography, No 26 (1992)) and SCALA (Acta Cryst D50: 760-763). The crystal initially diffracted to beyond 2.4 Å resolution, but radiation damage limited the final dataset resolution to 2.7 Å (Table 1).

The structure of turkey β₁AR-m23 was solved by molecular replacement with PHASER (McCoy et al (2007) J of App Cryst 40: 658-674), using the structure of human β₂AR (ref, PDB ID 2RH1) as an initial model. All four copies of the molecule in the triclinic unit cell were located. The amino acid sequence was corrected and the model was refined with PHENIX REFINE (Afonine et al (2005) CCP Newsletter, Contribution 8) and rebuilt with O (Jones et al (1991) Acta Cryst A47: 110-119). Tight non-crystallographic symmetry restraints (σ 0.025 Å) were applied to chains A and D and chains B and C. The cyanopindolol ligand, detergent and water molecules and the sodium ions were added at a late stage in the refinement. Final statistics are reported in Table 1.

TABLE 1 Crystal ID t1043 Space group P1 Cell dimensions a, b, c (Å) 55.5, 86.8, 95.5 α, β, γ (°) 67.6, 73.3, 85.8 Data Processing Resolution (Å) 45.1-2.7 R_(merge) 0.135 (0.666) <I/σ (I)> 5.8 (1.5) Completeness (%) 96.2 (95.7) Multiplicity 1.8 (1.8) Wilson B (Å²) 40.7 Refinement Rwork 0.226 Rfree 0.276 r.m.s. deviation bonds (Å) 0.011 r.m.s. deviation angles (°) 1.183

TABLE 2 Å Molecule A Water 2 Glu107 OE2 3.56 Na+ 2.49 Water 7 Trp101 O 3.04 Leu105 N 3.41 Water 8 Arg140 N 3.45 Phe139 N 3.18 Water 9 Thr136 O 3.21 Water 10 Ser165 O 3.19 Val164 O 3.17 Tyr199 OH 2.54 Water 11 Glu107 OE1 2.82 Trp174 NE1 2.74 Ile169 O 2.76 Arg175 NH2 3.19 Water 12 Arg197 NH1 2.83 Phe298 O 3.54 B/Arg149 NH2 3.54 Water 13 Cys285 O 2.86 Phe311 O 2.71 Phe289 N 2.7 Molecule B Water 12 Arg149 NH2 3.54 A/Arg197 NH1 2.83 A/Phe298 O 3.54 Water 14 Trp99 O 2.7 Gly102 N 2.85 Pro188 O 2.76 Water 15 Cys191 O 3.21 Thr110 OG1 2.77 Water 16 Arg197 N Water 17 Val303 N 2.83 Val303 O 3.39 Asn296 OD1 2.39 Water 18 Asn318 ND2 2.49 Trp286 NE1 3.21 Molecule C Water 19 Thr98 O 2.75 Leu100 N 3.02 Thr92 OG1 2.54 Water 20 Trp99 O 2.8 Pro188 O 2.85 Gly102 N 2.83 Water 21 Thr110 OG1 3.02 Water 22 Asp192 OD1 3.12 Gly189 O 3.46 Cys191 N 2.64 Water 23 Trp286 NE1 3.26 Asn318 ND2 3.09 Molecule D Water 6 Glu107 OE2 3.5 Na+ ion 2.68 Water 24 Trp101 O 2.7 Leu105 N 3.04 Water 25 Ile169 O 2.76 Trp174 NE1 2.65 Arg175 NH2 3.26 Glu107 OE1 2.88 Water 26 Gln186 OE1 3.38 Water 27 Thr110 OG1 3.21 Asp192 O 3.27 Water 28 Tyr199 OH 2.63 Ser165 O 2.92 Val164 O 3.35 Water 29 Phe311 O 2.84 Phe289 N 2.83 Cys285 O 2.65 Water 30 Gly315 O 2.43 Tyr316 O 3.37 Ser319 OG 2.99 Water 31 Asn322 ND2 3.43 Tyr326 OH 2.96 “27 water molecules in total, 8 in A, 6 in B, 5 in C and 9 in D” (one shared between A & B; water 12)

TABLE 3 Mutation Stability (wild type = 100) T144A 72 S145A 68 P146A 13 F147A 128 R148A 89 Y149A 1 Q150A 117 S151A 117

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EXAMPLE 2 Crystallisation of a Mutant Turkey β1-AR The Beta 36/m23 Crystallization Construct and Other Related Constructs

The Turkey beta-adrenergic receptor constructs Beta 34 and 36 are based on the previously described T34-424His6 construct [1], now renamed Beta 6. Beta 34 and 36, like Beta 6, are truncated at the N-terminus before residue 33, where the sequence MetGly has been added. Beta 34 & 36 are truncated at the C-terminus after Leu367, with the addition of a 6 histidine tag after the truncation. In Beta 36, two segments, comprising residues 244-271 and 277-278 of the third intracellular loop (ICL3) have also been deleted. All of the constructs incorporate the mutation C116L, which enhances expression [2]. Beta 34 and 36 both incorporate the mutation C358A, which eliminates the possibility of palmitoylation. The Beta 36/m23 crystallization construct includes in addition the six ‘m23’ mutations, R068S, M090V, Y227A, A282L, F327A and F338M, which enhance thermal/detergent stability [3]. Stabilized variants of Beta 6 (Beta 6/m23) and Beta 34 (Beta 34/m23) were also made by incorporating the six ‘m23’ mutations. A second version of Beta 36/m23 where C358 has not been mutated has also been made.

TABLE 4 Constructs. N-terminus C-terminus ICL 3 m23 Construct C116L truncated truncated deleted mutations C358A β6 Yes yes no no no no β34 Yes yes yes no no yes β36 Yes yes yes yes no yes β6/m23 Yes yes no no yes no β34/m23 Yes yes yes no yes yes β36/m23 Yes yes yes yes yes yes β36/m23/ yes yes yes yes yes no C358

Baculovirus Expression

The construct was expressed with the baculovirus system using Tni (High 5™) cells. The sequence CCCAAAATG was placed at the initiator methionine codon and the construct was subcloned into the baculovirus transfer vector pBacPAK8 (BD Clontech). The generation of recombinant baculovirus encoding Beta 36/m23 by co-transfection of Sf9 (S. frugiperda) cells, isolation of clonal virus, virus passage, and receptor expression in High 5™ cells were all as previously described [1].

Beta 36 and Beta 36/m23 Purification, General Description

Insect cell membranes were prepared and solubilized as described previously [1], except that for the Beta 36/m23 construct, decylmaltoside (1.5%) was substituted for dodecylmaltoside as the solubilizing detergent after it had been established that subsequent detergent exchange was inefficient if dodecylmaltoside was used.

Purification was with first two column steps described for the T34-424His6 (Beta 6) construct [1], IMAC (Nickel) and alprenolol sepharose, which were run overnight at 5° C. It was found that the final size exclusion step which had been used for Beta 6 was not necessary for the Beta 36 constructs.

Beta 36 and Beta 36/m23 purification was performed on a small/medium or large scale, with the solubilization of insect cell membranes from 1L, 2L or 4L culture volume respectively. In either case a 10 ml, 1.6 cm diameter IMAC (Ni sepharose FF) column was used for the first step, as described previously for purification on a 2-5 mg scale [1]. For the small/medium scale, purification was continued with a 2.5 ml (1.6 cm diameter) aiprenolol sepharose column, for the large scale purification a 6 ml (2.6 cm diameter) column was used. Detergent exchange was performed on the alprenolol sepharose column, bound receptor was washed with buffer containing the new detergent. The previously utilized high salt (1M NaCl) wash was not used because octylthioglucoside (OTG), the detergent into which the receptor was exchanged for crystallization, is insoluble in high ionic strength buffers. As OTG also sometimes crystallized at 5° C., the aiprenolol sepharose wash buffer, which was used during the overnight FPLC procedure was maintained at 30° C. Other buffers containing OTG were only used for a short time or were of lower ionic strength than the aiprenolol sepharose wash buffer, and therefore problems with detergent solubility were not encountered. It was also found that it was not in fact necessary to warm the aiprenolol sepharose column in order to enhance the elution of beta-1 adrenergic receptor with the competing ligand, a measure which is recommended for beta-2 adrenergic receptor chromatography [4]. Eluted receptor fractions were concentrated with 100 kDa molecular weight cut-off (mwco) centricon concentrators (Millipore) to 1-2 ml. A buffer exchange step was then performed on a desalting column in to achieve the required (low) buffer and salt concentrations for crystallization experiments.

Cyanopindolol is quite expensive (£50/mg) and poorly soluble in aqueous buffers (0.75 mM). In order to increase the ligand concentration for crystallization, whilst minimizing costs, concentrated receptor was diluted with a buffer containing 0.69 mM cyanopindolol and then re-concentrated. The procedure was then repeated before final concentration of the receptor to at least 5 mg/ml with a cyanopindolol concentration of at least 0.5 mM. When using other less expensive ligands, such as (−) alprenolol, the dilution and re-concentration steps could be circumvented as it was possible to simply exchange the receptor into a buffer containing the required final ligand concentration on the desalting column and then concentrate it.

Detailed Description of Chromatography and Subsequent Purification Steps, Purification for Crystallization in Octylthioglucoside

Buffer compositions are given in Table 5. Solubilized membrane proteins were applied to the 10 ml IMAC column at 0.35 ml/min. Total sample volumes were 60 ml, 120 ml or 180 ml for the purification of receptor from 1 L, 2L or 4L insect cells respectively. When sample loading was complete, the flow rate was increased to 1.85 ml/min and the column was washed with 80 ml IMAC A buffer. The imidazole concentration was increased to 27 mM (10% IMAC B buffer) with a linear gradient of 50 ml, and the column was further washed with 27 mM imidazole for 100 ml. The imidazole concentration was then rapidly increased to 250 mM (100% IMAC buffer) with a linear gradient of 20 ml, and elution was continued with 250 mM imidazole for a further 60 ml. Collection of a 65 ml volume which contained most of the receptor-1 binding activity was commenced as soon as the applied imidazole concentration had attained 150 mM. This partially-purified receptor fraction was then applied to a 2.5 ml, 1.6 cm diameter (1 or 2L scale purification) or 6 ml, 2.6 cm diameter (4L scale purification) alprenolol sepharose column.

Alprenolol Sepharose Chromatography, Small/Medium Scale (1-2L Cells)

The 2.5 ml alprenolol sepharose column was loaded at a flow-rate of 0.25 ml/min. When sample loading was complete, the bound active fraction of the receptor was washed with 50 ml of Alprenolol sepharose wash buffer at 0.25 ml/min. The procedure was then paused for 1 hour before elution, giving the receptor a total of 4 hours exposure to the new detergent before elution. Elution was effected with 10 ml alprenolol sepharose elution buffer (+cyanopindolol) followed by a further 10 ml elution buffer (−cyanopindolol), all at a flow-rate of 0.4 ml/min. The eluted receptor was recovered in a 15 ml volume. UV monitoring of receptor elution was not possible due to the high absorbance of the ligand.

Alprenolol Sepharose Chromatography, Large Scale (4L Cells)

The 6 ml, 2.6 cm diameter alprenolol sepharose column was loaded with partially purified receptor at 0.4 ml/min.

Receptor Concentration, Buffer Exchange and Centrifugation Prior to Crystallization

Eluted receptor fractions were first concentrated 10-fold with 100 kDa mwco centricons to 1-1.5 ml. A sample was taken for protein estimation so that an estimate of the final yield and the required final volume could be made. Buffer was then exchanged to PD-10 buffer by application of the receptor to a pre-equilibrated G-25 sephadex PD-10 desalting column (GE Healthcare). The eluted receptor (2.5 ml) was then further concentrated with 100 kDa mwco centricons to ˜200 μl. The receptor was then diluted with 250 μl dilution buffer, reconcentrated to ˜200 μl, and the dilution repeated. The receptor was finally reconcentrated to 5-10 mg/ml, recovered from the centricons and then centrifuged at 60,000 rpm for 10 minutes at 4° C. to remove any possible aggregates. After final protein estimation, the receptor concentration was adjusted by addition of dilution buffer if necessary to achieve a final concentration of 5.0-6.5 mg/ml for crystallization.

TABLE 5 Buffers used in receptor purifications Tris-HCl, Imidazole- Buffer pH 7.7 NaCl HCl, pH 8 EDTA Detergent Cyanopindolol³ IMAC A 20 mM 350 mM  2.5 mM 0 0.15% DecM 0 IMAC B 20 mM 350 mM 250 mM 0 0.15% DecM 0 Alp. Sepharose 20 mM 350 mM 0   1 mM  0.4% OTG² 0 wash Alp. sepharose 20 mM 350 mM 0 0.2 mM 0.35% OTG² 30 μM  elution¹ PD-10 exchange 10 mM  50 mM 0 0.1 mM 0.35% OTG² 2 μM buffer Cyanopindolol 10 mM  50 mM 0 0.1 mM 0.35% OTG² 0.69 mM   dilution buffer Size exclusion 20 mM  50 mM 0 0.5 mM 0.35% OTG² 2 μM DecM, decylmaltoside, OTG, octylthioglucoside ¹Alprenolol sepharose elution buffer was also prepared without cyanopindolol to continue elution of receptor, in order to minimize the quantity of ligand used ²Other detergents were also used for the later stages of purification, usually at a standard working concentration of 1.25 × cmc, eg fos-choline 10 (0.45%), hega 10 (0.35%) and nonylglucoside (0.28%) ³(-) alprenolol and other ligands were also used.

Exchange to Other Detergents

A variety of other detergents could be used for Beta 36/m23 purification. A working concentration of 1.25×cmc was used throughout in all buffers.

Size Exclusion Chromatography

Analytical size-exclusion chromatography was performed with on a Superdex 200 10/300 GL column. 100 μl samples were applied and run at 0.35 ml/min. The column was calibrated with the soluble protein standards ferritin (440 kDa), catalase (232 kDa), aldolase (158 kDa), BSA (67 kDa) and ovalbumin (43 kDa), which were run in the same buffer but without detergent. Preparative scale size-exclusion chromatography was performed with either a 16/60, for 1-4 mg receptor or with a 26/60 Superdex 200 column (4-10 mg receptor)

Size-exclusion chromatography was used as a final purification step in the preparation of Beta 6 and Beta 34 receptor constructs. When either of these constructs was eluted from a Superdex column, the main receptor peak, which was sharp and symmetrical, was preceded by smaller peaks comprising high molecular weight species which may have included aggregated receptor. When Beta 36 constructs were first purified, preparative size-exclusion chromatography was also used as a final purification step. However, a much improved elution profile was observed for Beta 36, along with an unusually late elution. Beta 36 also looked much cleaner on SDS PAGE when compared to both Beta 6 and Beta 34 constructs. For these reasons, size-exclusion chromatography was no longer considered to be a necessary step in the purification of Beta 36 constructs.

Analytical size-exclusion chromatography was routinely performed on Beta 36/m23 preparations as a quality control procedure and also to observe the effect on receptor properties after detergent exchange.

Apparent molecular weights of the Beta receptor constructs described were determined by size-exclusion chromatography on a calibrated column, as were the apparent molecular weights of Beta36/m23 in a variety of detergents. These results are listed in Table 6. Comparison of the apparent molecular weights of Beta 6, 34 & 36 in dodecylmaltoside with the predicted molecular weights of the respective constructs indicates that the behaviour of the Beta 36 construct has been dramatically altered, and it is possible that this is because the deletion of IC loop 3 has led to a reduced tendency to associate with itself and other proteins. When Beta 36/m23 was purified in the short-alkyl chain detergents which were used for crystallization, elution from the analytical size-exclusion column was later than when the receptor was eluted in dodecylmaltoside, indicating that the receptor was eluted in a detergent micelle which was significantly smaller (see FIG. 10). Because of the unusual behaviour of the Beta 36 construct, the apparent molecular weights of the receptor in these detergents was actually less than the calculated molecular weight of the construct.

TABLE 6 Size-exclusion data mwt. app Predicted Calculated with mwt. of construct detergent receptor in Construct mwt. (kDa) Detergent bound micelle¹ β6 45.06 C12-maltoside 120 122 β34 39.25 C12-maltoside 103 116 β36 35.95 C12-maltoside 79 112 β36/m23/C358 35.74 C10-maltoside 53 69 β36/m23 35.71 C10-maltoside 57.5 69 β36/m23 35.71 C9-maltoside 47.5 61.5 β36/m23 35.71 C9-glucoside 33.2 n/a β36/m23 35.71 C8-S-glucoside 28.1 n/a β36/m23 35.71 LDAO 64.3 n/a ¹The predicted weight of the receptor in the detergent micelle was calculated by addition of the molecular weight of the construct to the predicted mass of one detergent micelle; aggregation numbers for the respective detergents determined by the detergent manufacturer, Anatrace, were used to predict the following micellar masses: dodecylmaltoside, 77.6 kDa; decylmaltoside, 33.3 kDa; nonylmaltoside, 25.7 kDa.

Crystallization of Beta 36/m23

Crystallization was by the vapour diffusion method at 18° C. Receptor was diluted 1:1 with precipitant solution and crystallized on either MRC 96-well plates with the sitting drop method (200 nl or 500 nl receptor) or Qiagen easy xtal dg (dropguard) plates for hanging drops (1 μl receptor).

Beta 36/m23 purified in 0.35% OTG with 0.5 mM cyanopindolol crystallized over a wide pH range (5.6-9.5) and with a large variety of PEGs at concentrations of 25-35% as precipitant with the addition of wide range of salts. The best diffracting crystals with receptor purified in OTG were obtained with 0.1M ADA (N-(2-acetaimido) iminodiacetic acid) buffer, pH6.9-7.3 and 29-32% PEG 600 as precipitant. Crystals usually appeared within 24-48 hours, and crystal growth was complete within 72 hours. Initial crystal screening for crystallization conditions and the first rounds of optimization were with MRC sitting drop plates. However, crystals grown under hanging drop conditions on the Qiagen plates showed improved morphology and were easier to mount in cryoloops for freezing. Dropguard coverslips were used, the smaller of the two well sizes was appropriate for the 1 μl+1 μl drops. The use of the dropguard well restricted drop spreading and suppressed nucleation, possibly by restricting the surface area of the drop and slowing vapour diffusion. Larger crystals could be grown in this way than could be grown with either MRC sitting drop plates, sitting drops on microbridges, or conventional coverslips for hanging drops.

Diffracting crystals of Beta 36/m23 could also be grown with receptor purified in nonylglucoside, fos-choline 10 and hega 10, but crystallization conditions for these detergents have not so far been optimized. However, in all three cases the best conditions are in the pH range 7-8.5 with ˜30% PEG as precipitant.

Crystal Freezing and Cryoprotection

Crystals were mounted on Hampton CrystalCap HT™ loops and frozen with liquid nitrogen. It was presumed that the PEG 600 concentration in the crystallization drop was insufficient to give good cryoprotection, so the PEG concentration in the drop was increased to 70% in initial freezing attempts. As a variable unit cell size was observed, a cryoprotectant solution comprising either 40% PEG 600 or 35% PEG 600 and 5% glycerol was used in order to reduce variation of the unit cell due to dehydration of the crystal. Finally it was observed that it was not necessary to add any cryoprotectant to the drop, and many crystals were successfully frozen this way in order to preserve isomorphism. However, high resolution better than 3 Å was never seen in these crystals, therefore PEG concentrations of 50-70% were used for crystal freezing.

REFERENCES

-   [1] Warne, T, Chimside, J., and Schertler, G. F. (2003) Expression     and purification of truncated, non-glycosylated turkey     beta-adrenergic receptors for crystallization, Biochim. Biophys.     Acta. 1610, 133-40. -   [2] Parker, E. M., Kameyama, K., Higashijima, T. and     Ross, E. M. (1991) J. Biol. Chem. 266 (1), 519-27. -   [3] Serrano-Vega, M. J., Magnani, F., Shibata, Y.,     Tate, C. G. (2008) Proc Natl Accd Sci USA. 105 (3), 877-82 -   [4] Caron, M. G., Srinivasan, Y., Pitha, J., Kociolek, K. and     Lefkowitz, R. J. (1979) J. Biol. Chem. 254 (8), 2923-27.

EXAMPLE 3 RMSD Calculations A. Rmsd Calculation Between β2-AR Structures

RMSD Between PDB code: 2RH1 and PDB Code: 2R4S After LSQMAN Alignment (the 2R4S Structure is of Poor Quality and Low Resolution) (using only residues for alignment in H2-H6 as follows) Helix 2 69-90 (residue numbering from beta2)

Helix 3 109-134 Helix 4 148-164 Helix 5 200-229 Helix 6 269-291 Helix 7 311-323

Overall rmsd=0.74 Å on 384 main chain atoms, used in alignment (this large deviation is due almost entirely to inaccuracies in 2R4S)

Overall rmsd=1.38 Å on 552 main chain atoms, but many loops and uncertain regions were omitted in the 2R4S publication

Helix 1 1.01 Å on 63 atoms Helix 2 0.81 Å on 45 atoms

Helix 4 0.58 Å on 51 atoms

Helix 5 0.76 Å on 57 atoms Helix 6 0.43 Å on 66 atoms Helix 7 0.89 Å on 48 atoms Cytoplasmic loop-1 0.60 Å on 18 atoms Extracellular loop-1 1.09 Å on 42 atoms Cytoplasmic loop-2 1.25 Å on 30 atoms Extracellular loop-2 0.98 Å on 15 atoms Cytoplasmic loop-3 4.37 Å on 30 atoms Extracellular loop—no residues remain in the 2R4S in this region; none have been built Helix 8 3.10 Å on12 atoms

B. Rmsd Calculation Between β1-AR (Molecule B) and β2-AR

RMSD Between Beta1 molB and 2RH1 After LSQMAN Alignment (using residues only in H2-H6 for alignment as follows) Helix 2 69-90 (residue numbering from beta2)

Helix 3 109-134 Helix 4 148-164 Helix 5 200-229 Helix 6 269-291 Helix 7 311-323

Overall rmsd=0.399 Å on 426 main chain atoms (Cα, C, N) used in alignment in H2-H6

Overall rmsd=1.235 Å on 801 main chain atoms (Cα, C, N) in complete structure

Helix 1 0.606 Å on 63 atoms Helix 2 0.416 Å on 6 atoms Helix 3 0.304 Å on 78 atoms Helix 4 0.550 Å on 54 atoms Helix 5 0.401 Å on 90 atoms Helix 6 0.403 Å on 75 atoms Helix 7 0.310 Å on 63 atoms Cytoplasmic loop-1 0.796 Å on 27 atoms Extra cellular loop-1 0.732 Å on 54 atoms Cytoplasmic loop-2 4.830 Å on 39 atoms Extracellular loop-2 0.836 Å on 102 atoms Cytoplasmic loop-3 0.721 Å on 9 atoms Extracellular loop-3 0.985 Å on 27 atoms Helix 8 1.018 Å on 54 atoms

C. Rmsd Calculation Between β1-AR Molecules A and B

RMSD Between Beta1 molB and Beta1 molA After LSQMAN Alignment (alignment used only residues in H2-H6 as follows) Helix 2 69-90 (residue numbering from beta2)

Helix 3 109-134 Helix 4 148-164 Helix 5 200-229 Helix 6 269-291 Helix 7 311-323

Overall rmsd=0.314 Å on 426 main chain atoms in H2-H6 (Cα, C, N) used in alignment

Overall rmsd=0.465 Å on 792 main chain atoms from complete structure, excluding N-terminal part of H1.

Helix 1 2.185 Å on 63 atoms (all of H1—large because of the 60° kink of N-terminus before residue 42) Helix 2 0.312 Å on 6 atoms Helix 3 0.230 Å on 78 atoms Helix 4 0.388 Å on 54 atoms Helix 5 0.341 Å on 90 atoms Helix 6 0.230 Å on 75 atoms Helix 7 0.378 Å on 63 atoms Cytoplasmic loop-1 0.599 Å on 27 atoms Extracellular loop-1 0.418 Å on 54 atoms Cytoplasmic loop-2 0.468 Å on 39 atoms Extracellular loop-2 0.633 Å on 102 atoms Cytoplasmic loop-3 0.261 Å on 9 atoms (most of this very large loop deleted from coordinates) Extracellular loop-3 0.694 Å on 27 atoms Helix 8 0.510 Å on 54 atoms

D. RMSD Calculation Between β1-AR (Molecule B) and β2-AR (2RN1) Comparison of the Active Site Residues Between β1 and β2

B2 residue B1 residue B-W AA residue number number number Trp 109 117 3.28 Thr 110 118 3.29 Asp 113 121 3.32 Val 114 122 3.33 Val 117 125 3.36 Phe 193 201 5.32 Thr 195 203 5.34 Tyr 199 207 5.38 Ser 203 211 5.42 Ser 207 215 5.46 Phe 289 306 6.51 Phe 290 307 6.52 Asn 293 310 6.55 Asn 312 329 7.39

The β1 and β2 receptors were aligned based upon helices 2-7. The RMS difference between the position of the 14 ligand binding residues in β1 and β2 were then determined. For comparison, the RMS difference between the same residue in an alignment of β1 molecule A and β1 molecule B (molB) was performed.

Considering only Cα atoms, the RMSD between β1 molB and β2 is 0.4 Å compared to 0.2 Å when the two β1 molecules are compared.

Considering only side chain atoms, the RMSD between β1 molb and β2 is 0.6 Å compared to 0.3 Å when the two β1 molecules are compared.

Methods

The above rmsd calculations were performed using the following LSQMAN script:—

#!/bin/csh -f # # note that residue numbering here refers to human beta2 # sequence and homologous residues in beta1 # lsqman <<eof re BETA1 /ss1/rh15/MolB_bar_8feb08-lig-Na—H2O.pdb re BETA2 /ss1/rh15/2RH1_BAR_res.pdb li at ma ex BETA1 “A69-A90 A109-A134 A148-A165 A200-A229 A269-A293 A303-A323” BETA2 “A69 A109 A148 A200 A269 A303” at ca rmsd BETA1 “A109-A110 A113-A114 A117 A193 A195 A199 A203 A207 A289-290 A293 A312” BETA2 “A109 A113 A117 A193 A195 A199 A203 A207 A289 A293 A312” at ma rmsd BETA1 “A109-A110 A113-A114 A117 A193 A195 A199 A203 A207 A289-290 A293 A312” BETA2 “A109 A113 A117 A193 A195 A199 A203 A207 A289 A293 A312” at all rmsd BETA1 “A109-A110 A113-A114 A117 A193 A195 A199 A203 A207 A289-290 A293 A312” BETA2 “A109 A113 A117 A193 A195 A199 A203 A207 A289 A293 A312” at side rmsd BETA1 “A109-A110 A113-A114 A117 A193 A195 A199 A203 A207 A289-290 A293 A312” BETA2 “A109 A113 A117 A193 A195 A199 A203 A207 A289 A293 A312” quit eof #] Alignments and comparisons were obtained using LSQMAN: G. J. Kleywegt & T. A. Jones (1994). A super position.

CCP4/ESF-EACBM Newsletter on Protein Crystallography 31,

November 1994, pp. 9-14. [http://xray.bmc.uu.se/usf/factory_(—)4.html]

EXAMPLE 4

Turkey β1-AR is a member of the GPCR superfamily and its homology to many other known and potential drug targets can be used to build 3D models of such targets, which may also contain known ligands docked into the protein structure, by a process of homology modelling (Blundell et al (Eur. J. Biochem, Vol. 172, (1988), 513). These models can then be used in turn to select for binding partners, in particular small-molecule drug-like compounds, which are predicted to bind to the target in question. Such compounds are then either synthesised or, if they already exist and are available, tested for activity in biochemical or functional, assays. If they show the desired potency they may then be progressed for further screening, for example in in vivo pharmacology assays, or alternatively subjected to further rounds of chemistry or biosynthetic modification prior to testing in a succession of assays. In this fashion the turkey β1-AR structure can be used to enable the discovery of novel drug candidates.

Protein modelling is a well established technique that begins with an alignment of the target protein or its relevant orthologue (in this case GPCR with preferably but not necessarily >30% sequence identity across the transmembrane helical regions, for example human beta-1 adrenergic receptor, human beta-2 adrenergic receptor, human beta-3 adrenergic receptor, human dopamine D2 receptor, human muscarinic M1-M5 receptors, other aminergic receptors, human or rat neurotensin receptor, human adenosine Ata receptor) with β1-AR using an algorithm such as BLAST, preferably in the University of Washington implementation WU-BLAST (WU-BLAST version 2.0 executable programs for several UNIX platforms can be downloaded from ftp://blast. wustl. edu/blast/executables). This program is based on WU-BLAST version 1.4, which in turn is based on the public domain NCBI-BLAST version 1.4 (Altschul and Gish, 1996, Local alignment statistics, Doolittle ed., Methods in Enzymology 266: 460-480; Altschul et al., 1990, Basic local alignment search tool, Journal of Molecular Biology 215: 403-410; Gish and States, 1993, Identification of protein coding regions by database similarity search, Nature Genetics 3: 266-272; Karlin and Altschul, 1993, Applications and statistics for multiple high-scoring segments in molecular sequences, Proc. Natl. Acad. Sci. USA 90: 5873-5877.

In all search programs in the suite the gapped alignment routines are integral to the database search itself. Gapping can be turned off if desired. The default penalty (O) for a gap of length one is Q=9 for proteins and BLASTP, and Q=10 for BLASTN, but may be changed to any integer. The default per-residue penalty for extending a gap (R) is R=2 for proteins and BLASTP, and R=10 for BLASTN, but may be changed to any integer. Any combination of values for Q and R can be used in order to align sequences so as to maximize overlap and identity while minimizing sequence gaps. The default amino acid comparison matrix is BLOSUM62, but other amino acid comparison matrices such as PAM can be utilized.

Once the amino acid sequences of turkey β1-AR and the target protein of unknown structure have been aligned, the structures of the conserved amino acids in the structural representation of the turkey β1-AR may be transferred to the corresponding amino acids of the target protein. For example, a tyrosine in the amino acid sequence of turkey β1-AR may be replaced by a phenylalanine, the corresponding homologous amino acid in the amino acid sequence of the target protein.

The structures of amino acids located in non-conserved regions may be assigned manually by using standard peptide geometries or by molecular simulation techniques, such as molecular dynamics (Lee, M. R.; Duan, Y.; Kollman, P. A. State of the art in studying protein folding and protein structure prediction using molecular dynamics methods. Journal of Molecular Graphics & Modelling (2001), 19(1), 146-149). The final step in the process is accomplished by refining the entire structure using molecular dynamics and/or energy minimization. Typically, the predicted three dimensional structural representation will be one in which favourable interactions are formed within the target protein and/or so that a low energy conformation is formed.

Typically, homology modelling is performed using computer programs, for example SWISS MODEL available through the Swiss Institute for Bioinformatics in Geneva, Switzerland; WHATIF available on EMBL servers; Schnare et al. (1996) J. Mol. Biol, 256: 701-719; Blundell et al. (1987) Nature 326: 347-352; Fetrow and Bryant (1993) Bio/Technology 11:479-484; Greer (1991) Methods in Enzymology 202: 239-252; and Johnson et al (1994) Crit. Rev. Biochem. Mol. Biol. 29:1-68. An example of homology modelling is described in Szklarz G. D (1997) Life Sci. 61: 2507-2520.

Binding partners such as known agonists or antagonists, or molecules that may be agonists or antagonists, or simply molecules that it is thought may have the potential to interact with the receptor target can then be docked into the protein model, typically by positioning of a 3D representation of the candidate binding partner in the anticipated ligand binding region, by analogy with the cyanopindolol binding region delineated in the cyanopindolol/beta-1AR co-structure presented herein (Table A, B, C or D). Known or putative binding partners may then be modified stepwise, alternatively binding partners may be designed de novo using the empty or partly occupied binding site, or these two approaches may be combined.

In order to provide a three-dimensional structural representation of a candidate binding partner, the binding partner structural representation may be modelled in three dimensions using commercially available software for this purpose or, if its crystal structure is available, the coordinates of the structure may be used to provide a structural representation of the binding partner.

The design of binding partners that bind to a β1-AR or a model based on β1-AR generally involves consideration of two factors.

First, the binding partner must be capable of physically and structurally associating with parts or all of a β1-AR potential or known binding region or homologous parts of a modeled target receptor. Non-covalent molecular interactions important in this association include hydrogen bonding, van der Waals interactions, hydrophobic interactions and electrostatic interactions.

Second, the binding partner must be able to assume a conformation that allows it to associate with a binding region directly. Although certain portions of the binding partner will not directly participate in these associations, those portions of the binding partner may still influence the overall conformation of the molecule. This, in turn, may have a significant impact on potency. Such conformational requirements include the overall three-dimensional structure and orientation of the binding partner in relation to all or a portion of the binding region, or the spacing between functional groups of a binding partner comprising several binding partners that directly interact with the β1-AR or homologous target.

Thus it will be appreciated that selected coordinates which represent a binding region of the turkey β1-AR, e.g. atoms from amino acid residues contributing to the ligand binding site including amino acid residues 117, 118, 121, 122, 125, 201, 203, 207, 211, 215, 306, 307, 310 and 329 may be used. Additional preferences for the selected coordinates are as defined above with respect to the first aspect of the invention.

Designing of binding partners can generally be achieved in two ways, either by the step wise assembly of a binding partner or by the de novo synthesis of a binding partner.

With respect to the step-wise assembly of a binding partner, several methods may be used. Typically the process begins by visual inspection of, for example, any of the binding regions on a computer representation of the turkey β1-AR as defined by the coordinates in Table. A, Table B, Table C or Table D optionally varied within a rmsd of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof. Selected binding partners, or fragments or moieties thereof may then be positioned in a variety of orientations, or docked, within the binding region. Docking may be accomplished using software such as QUANTA and Sybyl (Tripos Associates, St. Louis, Mo.), followed by, or performed simultaneously with, energy minimization, rigid-body minimization (Gshwend, supra) and molecular dynamics with standard molecular mechanics force fields, such as CHARMM and AMBER.

Specialized computer programs may also assist in the process of selecting binding partners or fragments or moieties thereof. These include: 1. GRID (P. J. Goodford, “A Computational Procedure for Determining Energetically Favorable Binding Sites on Biologically Important Macromolecules”, J. Med. Chem., 28, pp. 849-857 (1985)). GRID is available from Oxford University, Oxford, UK. 2. MCSS (A. Miranker et al., “Functionality Maps of Binding Sites: A Multiple Copy Simultaneous Search Method.” Proteins: Structure, Function and Genetics, 11, pp. 29-34 (1991)). MCSS is available from Molecular Simulations, San Diego, Calif. 3. AUTODOCK (D. S. Goodsell et al., “Automated Docking of Substrates to Proteins by Simulated Annealing”, Proteins: Structure, Function, and Genetics, 8, pp. 195-202 (1990)). AUTODOCK is available from Scripps Research Institute, La Jolla, Calif. 4. DOCK (I. D. Kuntz et al., “A Geometric Approach to Macromolecule-Ligand Interactions”, J. Mol. Biol., 161, pp. 269-288 (1982)). DOCK is available from University of California, San Francisco, Calif.

Once suitable binding partners or fragments have been selected, they may be assembled into a single compound or complex. Assembly may be preceded by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates of the turkey β1-AR or a model of an homologous target. This would be followed by manual model building using software such as QUANTA or Sybyl.

Useful programs to aid one of skill in the art in connecting the individual chemical entities or fragments include: 1. CAVEAT (P. A. Bartlett et al., “CAVEAT: A Program to Facilitate the Structure-Derived Design of Biologically Active Molecules”, in “Molecular Recognition in Chemical and Biological Problems”, Special Pub., Royal Chem. Soc., 78, pp. 182-196 (1989); G. Lauri and P. A. Bartlett, “CAVEAT: a Program to Facilitate the Design of Organic Molecules”, J. Comput. Aided Mol. Des., 8, pp. 51-66 (1994)). CAVEAT is available from the University of California, Berkeley, Calif.; 2. 3D Database systems such as ISIS (MDL Information Systems, San Leandro, Calif.). This area is reviewed in Y. C. Martin, “3D Database Searching in Drug Design”, J. Med. Chem., 35, pp. 2145-2154 (1992); and 3. HOOK (M. B. Eisen et al., “HOOK: A Program for Finding Novel Molecular Architectures that Satisfy the Chemical and Steric Requirements of a Macromolecule Binding Site”, Proteins: Struct., Funct., Genet., 19, pp. 199-221 (1994). HOOK is available from Molecular Simulations, San Diego, Calif.

Thus the invention includes a method of designing a binding partner of a β1-AR or an homologous target model comprising the steps of: (a) providing a structural representation of a β1-AR binding region as defined by the coordinates of turkey β1-AR of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å or selected coordinates thereof (b) using computational means to dock a three dimensional structural representation of a first binding partner in part of the binding region; (c) docking at least a second binding partner in another part of the binding region; (d) quantifying the interaction energy between the first or second binding partner and part of the binding region; (e) repeating steps (b) to (d) with another first and second binding partner, selecting a first and a second binding partner based on the quantified interaction energy of all of said first and second binding partners; (f) optionally, visually inspecting the relationship of the first and second binding partner to each other in relation to the binding region; and (g) assembling the first and second binding partners into a one binding partner that interacts with the binding region by model building.

As an alternative to the step-wise assembly of binding partners, binding partners may be designed as a whole or “de novo” using either an empty binding region or optionally including some portion(s) of a known binding partner(s). There are many de novo ligand design methods including: 1. LUDI (H.-J. Bohm, “The Computer Program LUDI: A New Method for the De Novo Design of Enzyme Inhibitors”, J. Comp. Aid. Molec. Design, 6, pp. 61-78 (1992)). LUDI is available from Molecular Simulations Incorporated, San Diego, Calif.; 2. LEGEND (Y. Nishibata et al., Tetrahedron, 47, p. 8985 (1991)). LEGEND is available from Molecular Simulations Incorporated, San Diego, Calif.; 3. LeapFrog (available from Tripos Associates, St. Louis, Mo.); and 4. SPROUT (V. Gillet et al., “SPROUT: A Program for Structure Generation)”, J. Comput. Aided Mol. Design, 7, pp. 127-153 (1993)). SPROUT is available from the University of Leeds, UK.

Other molecular modelling techniques may also be employed in accordance with this invention (see, e.g., N. C. Cohen et al., “Molecular Modeling Software and Methods for Medicinal Chemistry, J. Med. Chem., 33, pp. 883-894 (1990); see also, M. A. Navia and M. A. Murcko, “The Use of Structural Information in Drug Design”, Current Opinions in Structural Biology, 2, pp. 202-210 (1992); L. M. Balbes et al., “A Perspective of Modern Methods in Computer-Aided Drug Design”, in Reviews in Computational Chemistry, Vol. 5, K. B. Lipkowitz and D. B. Boyd, Eds., VCH, New York, pp. 337-380 (1994); see also, W. C. Guida, “Software For Structure-Based Drug Design”, Curr. Opin. Struct. Biology, 4, pp. 777-781 (1994)).

In addition to the methods described above in relation to the design of binding partners, other computer-based methods are available to select for binding partners that interact with β1-AR.

For example the invention involves the computational screening of small molecule databases for binding partners that can bind in whole, or in part, to the turkey β1-AR or an homologous target model. In this screening, the quality of fit of such binding partners to a binding region of a β1-AR site as defined by the coordinates of turkey β1-AR of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å or selected coordinates thereof, may be judged either by shape complementarity or by estimated interaction energy (E. C. Meng et al., J. Comp. Chem., 13, pp. 505-524 (1992)).

For example, selection may involve using a computer for selecting an orientation of a binding partner with a favourable shape complementarity in a binding region comprising the steps of: (a) providing the coordinates of turkey β1-AR of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å or selected coordinates thereof and a three-dimensional structural representation of one or more candidate binding partners; (b) employing computational means to dock a first binding partner in the binding region; (c) quantitating the contact score of the binding partner in different orientions; and (d) selecting an orientation with the highest contact score.

The docking may be facilitated by the contact score. The method may further comprise the step of generating a three-dimensional structural repsentation of the binding region and binding partner bound therein prior to step (b).

The method may further, comprise the steps of: (e) repeating steps (b) through (d) with a second binding partner; and (f) selecting at least one of the first or second binding partner that has a higher contact score based on the quantitated contact score of the first or second binding partner.

In another embodiment, selection may involve using a computer for selecting an orientation of a binding partner that interacts favourably with a binding region comprising; a) providing the coordinates of turkey β1-AR of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å or selected coordinates thereof; b) employing computational means to dock a first binding partner in the binding region; c) quantitating the interaction energy between the binding partner and all or part of a binding region for different orientations of the binding partner; and d) selecting the orientation of the binding partner with the most favorable interaction energy.

The docking may be facilitated by the quantitated interaction energy and energy minimization with or without molecular dynamics simulations may be performed simultaneously with or following step (b).

The method may further comprise the steps of: (e) repeating steps (b) through (d) with a second binding partner; and (f) selecting at least one of the first or second binding partner that interacts more favourably with a binding region based on the quantitated interaction energy of the first or second binding partner.

In another embodiment, selection may involve screening a binding partner to associate at a deformation energy of binding of less than −7 kcal/mol with a β1-AR binding region comprising: (a) providing the coordinates of turkey β1-AR of Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å or selected coordinates thereof and employing computational means which utilise coordinates to dock the binding partner into a binding region; (b) quantifying the deformation energy of binding between the binding partner and the binding region; and (d) selecting a binding partner that associates with a β1-AR binding region at a deformation energy of binding of less than −7 kcal/mol.

The potential binding effect of a binding partner on β1-AR may be analysed prior to its actual synthesis and testing by the use of computer modeling techniques. If the theoretical structure of the given entity suggests insufficient interaction and association between it and the β1-AR, testing of the entity is obviated. However, if computer modelling indicates a strong interaction, the molecule may then be synthesized and tested for its ability to bind to a β1-AR. In this manner, synthesis of inoperative compounds may be avoided.

The compound is then tested in a physical drug screen such as a radioligand binding assay, a fluorescent ligand binding assay, a whole cell functional assay for example by measuring cAMP upregulation, or a large range of other possible assays well known to those skilled in the art. The choice of assay is highly dependent on the target GPCR.

Once drug-like hit or lead molecules have been identified they may be modified by iterative medicinal chemistry. Co-crystallisation or soaking of crystals of turkey beta-1 AR with these “leads” would be a useful guide to their binding modes, and such information is fed into molecular modeling and design as described at the start of this Example (Example 4).

Binding surfaces for macromolecules, for example G-proteins or antibodies, might also be predicted using the structure of beta-1 AR or of homology models based on it.

Tables A-D

Tables A-D show the x, y and z coordinates by amino acid residue of each non-hydrogen atom in the polypeptide structure for molecules A, B, C and D respectively, in addition to the antagonist cyanopindolol atoms. The fourth column indicates whether the atom is from an amino acid residue of the protein (by 3-letter amino acid code eg TRP, GLU, ALA etc), the cyanopindolol ligand (PDL), a sodium atom (NA), a water molecule (HOH), octyithioglucoside molecule (8TG)¹ or a decylmaltoside atom (DMU)¹ (¹Molecule D only).

Parameters used in the modelling of the turkey β1-AR are provided below:

REMARK  Date 2008-02-08 Time 12:58:22 GMT +0000 REMARK PHENIX refinement REMARK ****************** SUMMARY OF INPUT REFLECTION DATA ****************** REMARK Reflections: REMARK  file name  :bar_t1043_a_trunc_201to1040_27A_unique1.mtz REMARK  labels :[‘F_bar_t1043, SIGF_bar_t1043, DANO, SIGDANO’] REMARK  resolution d_max   :45.1367 A REMARK  resolution d_min  :2.7001 A REMARK  number of reflections total :72699 REMARK  number of reflections work  :69129 (percent from total = 95.09) REMARK  number of reflections test :3570 (percent from total = 4.91) REMARK  completeness :0.8391 (in range: 45.1367-2.7001 A) REMARK R-free flags: REMARK  file name  :bar_t1043_a_trunc_201to1040_27A_unique1.mtz REMARK  label :FreeR_flag REMARK  test_flag_value: 1 REMARK Experimental phase information: Not available REMARK *********************** SUMMARY OF INPUT MODEL *********************** REMARK Model file name(s): REMARK  /andrewgrp0/andrew/gpcr/bar/esrf_7dec07/rebuild_8feb.pdb REMARK Number of atoms  :8913 REMARK Unit cell volume :407066.316 REMARK Space group :1 (P 1) REMARK Number of symmetries : 1 REMARK |-ADP statistics (Wilson B = 38.602)------------------------------| REMARK |Atom |Number of | isotropic or equivalent| Anisotropy |min/max | REMARK |type |iso  aniso |min  max  mean | min max mean | REMARK |------|---------|--------------|------------| REMARK |Solv+Mac: 8913 0  10.55 170.05 46.37 None None None | REMARK |Sol.  :27 0 40.00 40.00 40.00 None None None | REMARK |Mac.  :8886 0  10.55 170.05 46.39 None None None | REMARK |Hyd.  :0 0  None None None None None None | REMARK |------------------------------------------- | REMARK | Distribution of isotropic (or equivalent) ADP for non-H atoms:| REMARK |Bin#  value range  #atoms | Bin#  value range  #atoms | REMARK | 0: 10.550-26.500: 1339 | 5:  90.300-106.250: 320 | REMARK | 1: 26.500-42.450: 3750 | 6: 106.250-122.200: 158 | REMARK | 2: 42.450-58.400: 1834 | 7: 122.200-138.150:  91 | REMARK | 3: 58.400-74.350: 857 | 8: 138.150-154.100:  27 | REMARK | 4: 74.350-90.300: 533 | 9: 154.100-170.050:  4 | REMARK |     =>continue=>     | REMARK |-------------------------------------------------------------| REMARK |-Geometry statistics-----------------------------------| REMARK |Type | Deviation from ideal | Targets |Target (sum) | REMARK |  | mean  max min|  |   | REMARK |bond | 0.025 0.820 0.000| 9858.434|   | REMARK |angle | 2.000 70.460 0.000| 8178.315|   | REMARK |chirality| 0.090 0.413 0.000| 295.520| 28592.299 | REMARK |planarity| 0.019 0.340 0.000| 2731.746|   | REMARK |dihedral|25.199 174.976 0.001| 5701.449 |   | REMARK |nonbonded| 4.533 5.540 1.491| 1826.836 |   | REMARK |------------------------------------------------| REMARK |------------------------------------------------| REMARK |  Histogram of deviations from ideal values for  | REMARK |Bonds    |Angles    |Nonbonded contacts| REMARK |0.000-0.082: 9080| 0.000-7.046: 12340|1.491-1.896:   3| REMARK |0.082-0.164:  9| 7.046-14.092: 59|1.896-2.301:   12| REMARK |0.164-0.246:  7| 14.092-21.138:  4|2.301-2.706:  456| REMARK |0.246-0.328:  7| 21.138-28.184:  0|2.706-3.110: 7093| REMARK |0.328-0.410:  5| 28.184-35.230:  0|3.110-3.515: 8679| REMARK |0.410-0.492:  9| 35.230-42.276:  0|3.515-3.920: 14282| REMARK |0.492-0.574:  0| 42.276-49.322:  0|3.920-4.325: 15158| REMARK |0.574-0.656:  0| 49.322-56.368:  0|4.325-4.730: 21695| REMARK |0.656-0.738:  0| 56.368-63.414:  0|4.730-5.135: 24834| REMARK |0.738-0.820:  2| 63.414-70.460:  4|5.135-5.540: 27926| REMARK |--------------------------------------| REMARK ******************** REFINEMENT SUMMARY: QUICK FACTS ******************** REMARK Start: r_work = 0.2422 r_free = 0.2792 bonds = 0.025 angles = 2.000 REMARK Final: r_work = 0.2264 r_free = 0.2759 bonds = 0.011 angles = 1.183 REMARK ********************************************************************** REMARK Refinement target : ml REMARK Calculation algorithm :fft REMARK Use sin/cos table :False REMARK Statistics in bins for work reflections: REMARK  Bin Resolution Compl. No. Scale_k1(work) R-factor(work) REMARK  number range   refl. REMARK  1: 45.1430-13.8198 0.77 474 0.507 0.3670 REMARK  2: 13.8198-11.0217 0.86 541 0.431 0.2138 REMARK  3: 11.0217-9.6440 0.83 518 0.419 0.1873 REMARK  4: 9.6440-8.7693 0.83 533 0.423 0.1731 REMARK  5: 8.7693-8.1447 0.85 551 0.419 0.1710 REMARK  6: 8.1447-7.6669 0.79 480 0.414 0.1828 REMARK  7: 7.6669-7.2846 0.81 513 0.402 0.2505 REMARK  8: 7.2846-6.9687 0.86 523 0.390 0.2300 REMARK  9: 6.9687-6.7013 0.84 528 0.384 0.2409 REMARK  10: 6.7013-6.4708 0.81 537 0.390 0.2345 REMARK  11: 6.4708-6.2690 0.83 483 0.397 0.2555 REMARK  12: 6.2690-6.0902 0.80 519 0.390 0.2314 REMARK  13: 6.0902-5.9302 0.84 520 0.386 0.2375 REMARK  14: 5.9302-5.7859 0.83 555 0.391 0.2266 REMARK  15: 5.7859-5.6546 0.82 483 0.388 0.2331 REMARK  16: 5.6546-5.5345 0.83 502 0.396 0.2144 REMARK  17: 5.5345-5.4239 0.78 517 0.397 0.2102 REMARK  18: 5.4239-5.3217 0.81 511 0.406 0.2178 REMARK  19: 5.3217-5.2268 0.82 507 0.421 0.1957 REMARK  20: 5.2268-5.1384 0.81 532 0.414 0.1925 REMARK  21: 5.1384-5.0556 0.79 433 0.425 0.1947 REMARK  22: 5.0556-4.9779 0.79 525 0.428 0.1900 REMARK  23: 4.9779-4.9048 0.81 531 0.442 0.1859 REMARK  24: 4.9048-4.8358 0.83 497 0.434 0.1702 REMARK  25: 4.8358-4.7705 0.80 483 0.445 0.1860 REMARK  26: 4.7705-4.7086 0.83 564 0.452 0.1787 REMARK  27: 4.7086-4.6498 0.82 481 0.461 0.1718 REMARK  28: 4.6498-4.5938 0.82 489 0.467 0.1841 REMARK  29: 4.5938-4.5405 0.83 544 0.460 0.1638 REMARK  30: 4.5405-4.4895 0.81 551 0.467 0.1795 REMARK  31: 4.4895-4.4408 0.81 485 0.479 0.1827 REMARK  32: 4.4408-4.3941 0.80 501 0.473 0.1807 REMARK  33: 4.3941-4.3493 0.84 512 0.477 0.1683 REMARK  34: 4.3493-4.3062 0.82 497 0.482 0.2027 REMARK  35: 4.3062-4.2649 0.81 516 0.473 0.1830 REMARK  36: 4.2649-4.2250 0.81 504 0.477 0.1708 REMARK  37: 4.2250-4.1866 0.78 513 0.474 0.1919 REMARK  38: 4.1866-4.1496 0.83 487 0.492 0.1905 REMARK  39: 4.1496-4.1139 0.82 533 0.487 0.1658 REMARK  40: 4.1139-4.0793 0.79 526 0.479 0.1790 REMARK  41: 4.0793-4.0459 0.80 468 0.461 0.2039 REMARK  42: 4.0459-4.0136 0.82 537 0.476 0.1710 REMARK  43: 4.0136-3.9822 0.85 479 0.487 0.1784 REMARK  44: 3.9822-3.9519 0.85 527 0.482 0.1788 REMARK  45: 3.9519-3.9224 0.77 525 0.475 0.1845 REMARK  46: 3.9224-3.8938 0.80 527 0.476 0.1793 REMARK  47: 3.8938-3.8660 0.78 491 0.474 0.1935 REMARK  48: 3.8660-3.8390 0.81 489 0.464 0.1744 REMARK  49: 3.8390-3.8127 0.83 518 0.474 0.1729 REMARK  50: 3.8127-3.7871 0.78 488 0.473 0.1796 REMARK  51: 3.7871-3.7622 0.80 492 0.473 0.1835 REMARK  52: 3.7622-3.7379 0.85 553 0.453 0.1781 REMARK  53: 3.7379-3.7143 0.83 499 0.465 0.1802 REMARK  54: 3.7143-3.6912 0.81 486 0.463 0.1792 REMARK  55: 3.6912-3.6687 0.79 505 0.467 0.1779 REMARK  56: 3.6687-3.6468 0.80 531 0.460 0.1919 REMARK  57: 3.6468-3.6253 0.79 468 0.464 0.1954 REMARK  58: 3.6253-3.6044 0.83 569 0.460 0.1950 REMARK  59: 3.6044-3.5839 0.83 524 0.450 0.2064 REMARK  60: 3.5839-3.5639 0.81 485 0.456 0.1803 REMARK  61: 3.5639-3.5443 0.80 479 0.454 0.2114 REMARK  62: 3.5443-3.5252 0.81 534 0.436 0.2086 REMARK  63: 3.5252-3.5064 0.82 485 0.447 0.2267 REMARK  64: 3.5064-3.4881 0.80 533 0.445 0.2026 REMARK  65: 3.4881-3.4701 0.80 446 0.445 0.2176 REMARK  66: 3.4701-3.4525 0.79 507 0.443 0.2202 REMARK  67: 3.4525-3.4353 0.79 519 0.438 0.2234 REMARK  68: 3.4353-3.4183 0.77 486 0.442 0.2201 REMARK  69: 3.4183-3.4018 0.78 494 0.439 0.2056 REMARK  70: 3.4018-3.3855 0.80 513 0.432 0.2028 REMARK  71: 3.3855-3.3695 0.83 554 0.420 0.2303 REMARK  72: 3.3695-3.3539 0.80 506 0.435 0.2238 REMARK  73: 3.3539-3.3385 0.83 478 0.436 0.2589 REMARK  74: 3.3385-3.3234 0.79 469 0.436 0.2351 REMARK  75: 3.3234-3.3086 0.81 505 0.436 0.2252 REMARK  76: 3.3086-3.2940 0.78 492 0.431 0.2556 REMARK  77: 3.2940-3.2797 0.79 494 0.436 0.2206 REMARK  78: 3.2797-3.2656 0.82 524 0.437 0.2250 REMARK  79: 3.2656-3.2518 0.78 502 0.439 0.2313 REMARK  80: 3.2518-3.2382 0.83 554 0.428 0.2364 REMARK  81: 3.2382-3.2248 0.80 461 0.417 0.2308 REMARK  82: 3.2248-3.2116 0.78 486 0.423 0.2364 REMARK  83: 3.2116-3.1987 0.77 486 0.428 0.2450 REMARK  84: 3.1987-3.1859 0.79 509 0.436 0.2354 REMARK  85: 3.1859-3.1734 0.76 498 0.423 0.2426 REMARK  86: 3.1734-3.1611 0.80 494 0.424 0.2308 REMARK  87: 3.1611-3.1489 0.81 553 0.416 0.2461 REMARK  88: 3.1489-3.1369 0.75 449 0.424 0.2294 REMARK  89: 3.1369-3.1251 0.82 505 0.417 0.2370 REMARK  90: 3.1251-3.1135 0.77 452 0.411 0.2345 REMARK  91: 3.1135-3.1021 0.78 449 0.414 0.2380 REMARK  92: 3.1021-3.0908 0.79 466 0.414 0.2603 REMARK  93: 3.0908-3.0797 0.78 515 0.406 0.2378 REMARK  94: 3.0797-3.0687 0.79 529 0.407 0.2376 REMARK  95: 3.0687-3.0579 0.78 512 0.423 0.2520 REMARK  96: 3.0579-3.0473 0.80 526 0.407 0.2527 REMARK  97: 3.0473-3.0368 0.81 496 0.398 0.2465 REMARK  98: 3.0368-3.0264 0.80 493 0.400 0.2503 REMARK  99: 3.0264-3.0162 0.80 486 0.403 0.2406 REMARK 100: 3.0162-3.0061 0.79 509 0.405 0.2662 REMARK 101: 3.0061-2.9962 0.80 472 0.410 0.2533 REMARK 102: 2.9962-2.9863 0.79 507 0.413 0.2550 REMARK 103: 2.9863-2.9767 0.82 509 0.415 0.2555 REMARK 104: 2.9767-2.9671 0.82 525 0.403 0.2507 REMARK 105: 2.9671-2.9576 0.76 518 0.389 0.2509 REMARK 106: 2.9576-2.9483 0.81 501 0.391 0.2681 REMARK 107: 2.9483-2.9391 0.78 452 0.403 0.2776 REMARK 108: 2.9391-2.9300 0.79 461 0.400 0.2547 REMARK 109: 2.9300-2.9210 0.78 473 0.411 0.2655 REMARK 110: 2.9210-2.9121 0.76 512 0.406 0.2775 REMARK 111: 2.9121-2.9034 0.78 462 0.402 0.2802 REMARK 112: 2.9034-2.8947 0.80 522 0.400 0.2794 REMARK 113: 2.8947-2.8861 0.79 538 0.398 0.2835 REMARK 114: 2.8861-2.8777 0.78 481 0.397 0.2668 REMARK 115: 2.8777-2.8693 0.80 501 0.399 0.2632 REMARK 116: 2.8693-2.8611 0.77 481 0.384 0.2565 REMARK 117: 2.8611-2.8529 0.79 532 0.404 0.2903 REMARK 118: 2.8529-2.8448 0.79 476 0.403 0.2808 REMARK 119: 2.8448-2.8368 0.75 492 0.392 0.2642 REMARK 120: 2.8368-2.8289 0.80 491 0.380 0.2620 REMARK 121: 2.8289-2.8211 0.80 469 0.395 0.2657 REMARK 122: 2.8211-2.8134 0.80 467 0.395 0.2819 REMARK 123: 2.8134-2.8057 0.79 492 0.414 0.2939 REMARK 124: 2.8057-2.7982 0.80 499 0.401 0.2750 REMARK 125: 2.7982-2.7907 0.81 551 0.392 0.3078 REMARK 126: 2.7907-2.7833 0.77 499 0.387 0.3175 REMARK 127: 2.7833-2.7760 0.77 452 0.390 0.3239 REMARK 128: 2.7760-2.7687 0.77 449 0.397 0.3138 REMARK 129: 2.7687-2.7615 0.75 509 0.399 0.3012 REMARK 130: 2.7615-2.7544 0.77 487 0.389 0.3305 REMARK 131: 2.7544-2.7474 0.77 477 0.392 0.3205 REMARK 132: 2.7474-2.7405 0.74 474 0.406 0.3250 REMARK 133: 2.7405-2.7336 0.76 431 0.396 0.3534 REMARK 134: 2.7336-2.7268 0.73 515 0.394 0.3721 REMARK 135: 2.7268-2.7200 0.73 439 0.393 0.3536 REMARK 136: 2.7200-2.7133 0.76 480 0.402 0.3558 REMARK 137: 2.7133-2.7067 0.72 455 0.411 0.3558 REMARK 138: 2.7067-2.7002 0.73 470 0.443 0.3594 REMARK  where: REMARK  R-factor = SUM(||Fobs|−Scale_k1 * |Fmodel||)/SUM(|Fobs|) REMARK  Scale_k1 = SUM(|Fobs| * |Fmodel|)/SUM(|Fmodel|**2) REMARK  Fmodel = fb_cart * (Fcalc + Fbulk) REMARK  Fbulk = k_sol * exp(−b_sol * s**2/4) * Fmask REMARK  Fcalc = structure factors calculated from atomic model REMARK  fb_cart = exp(−h(t) * A(−1) * B_cart * A(−1t) * h), REMARK  A - orthogonalization matrix REMARK |−ADP statistics (Wilson B = 38.602)--------------------| REMARK | Atom | Number of | Isotropic or equivalent| Anisotropy |min/max | REMARK | type |iso aniso | min max mean | min max mean | REMARK | ----|-------|-------------|-------------| REMARK | Solv+Mac: 8913 0  11.29 162.50 46.52 None None None | REMARK | Sol. :27 0  13.55 60.94 33.46 None None None | REMARK | Mac. :8886 0  11.29 162.50 46.56 None None None | REMARK | Hyd. :0 0  None None None None None None | REMARK | ------------------------------------------------ | REMARK | Distribution of isotropic (or equivalent) ADP for non-H atoms: | REMARK | Bin#  value range  #atoms | Bin#  value range  #atoms | REMARK | 0: 11.293-26.413: 1281 | 5: 86.894-102.015: 347 | REMARK | 1: 26.413-41.533: 3688 | 6: 102.015-117.135: 200 | REMARK | 2: 41.533-56.654: 1823 | 7: 117.135-132.255: 108 | REMARK | 3: 56.654-71.774: 837 | 8: 132.255-147.375: 62 | REMARK | 4: 71.774-86.894: 554 | 9: 147.375-162.496: 13 | REMARK |     =>continue=>     | REMARK |-------------------------------------------------------------| REMARK |-Geometry statistics-----------------------------------| REMARK |Type | Deviation from ideal | Targets |Target (sum) | REMARK |  | mean  max min |   |   | REMARK |bond | 0.011 0.380 0.000| 914.190|    | REMARK |angle | 1.183 11.356 0.000| 3117.897|    | REMARK |chirality| 0.075 0.374 0.000 | 204.632| 10760.461 | REMARK |planarity| 0.005 0.048 0.000| 190.107|    | REMARK |dihedral | 25.170 170.893 0.007| 5289.495|    | REMARK |nonbonded| 4.315 5.475 2.231| 1044.139|    | REMARK |------------------------------------------------| REMARK |------------------------------------------------| REMARK |   Histogram of deviations from ideal values for   | REMARK |Bonds   |Angles    |Nonbonded contacts| REMARK |0.000-0.038: 9102| 0.000-1.136: 9825|2.231-2.555: 43| REMARK |0.038-0.076:  5| 1.136-2.271: 1815|2.555-2.880: 3490| REMARK |0.076-0.114:  2| 2.271-3.407: 477|2.880-3.204: 5853| REMARK |0.114-0.152:  0| 3.407-4.543: 179|3.204-3.529: 7001| REMARK |0.152-0.190:  4| 4.543-5.678:  69|3.529-3.853: 11830| REMARK |0.190-0.228:  3| 5.678-6.814:  25|3.853-4.177: 10222| REMARK |0.228-0.266:  1|6.814-7.949:  7|4.177-4.502: 16163| REMARK |0.266-0.304:  0|7.949-9.085:  7|4.502-4.826: 18060| REMARK |0.304-0.342:  1|9.085-10.221:  1|4.826-5.151: 20389| REMARK |0.342-0.380:  1|10.221-11.356:  2|5.151-5.475: 4494| REMARK |------------------------------------------------| REMARK ****************** REFINEMENT STATISTICS STEP BY STEP ****************** REMARK leading digit, like 1_, means number of macro-cycle REMARK 0 :statistics at the very beginning when nothing is done yet REMARK 1_bss: bulk solvent correction and/or (anisotropic) scaling REMARK 1_xyz: refinement of coordinates REMARK 1_adp: refinement of ADPs (Atomic Displacement Parameters) REMARK 1_sar: simulated annealing refinement of x, y, z REMARK ------------------------------------------------------------- REMARK R-factors, x-ray target values and norm of gradient of x-ray target REMARK stage r-work r-free xray_target_w xray_target_t REMARK  0 :0.3647 0.3686 4.744063e+00 4.810621e+00 REMARK  1_bss: 0.2422 0.2792 4.652633e+00 4.733425e+00 REMARK  1_xyz: 0.2264 0.2812 4.617832e+00 4.733139e+00 REMARK  1_adp: 0.2226 0.2783 4.601622e+00 4.723398e+00 REMARK  2_bss: 0.2233 0.2754 4.601172e+00 4.717059e+00 REMARK  2_xyz: 0.2287 0.2762 4.615511e+00 4.716959e+00 REMARK  2_sar: 0.2292 0.2757 4.617258e+00 4.717022e+00 REMARK  2_xyz: 0.2277 0.2765 4.613917e+00 4.717557e+00 REMARK  2_adp: 0.2261 0.2767 4.609129e+00 4.717554e+00 REMARK  3_bss: 0.2258 0.2762 4.608872e+00 4.717243e+00 REMARK  3_xyz: 0.2266 0.2761 4.610807e+00 4.716857e+00 REMARK  3_adp: 0.2268 0.2764 4.610185e+00 4.716700e+00 REMARK  3_bss: 0.2264 0.2759 4.610043e+00 4.716476e+00 REMARK ------------------------------------------------------------- REMARK Weights for target T = Exray * wxc * wxc_scale + Echem * wc and REMARK angles between gradient vectors, eg. (d_Exray/d_sites, d_Echem/d_sites) REMARK stage   wxc  wxu wxc_sc wxu_sc /_gxc, gc /_gxu, gu REMARK  0 : 1.1624e+01 1.9406e−01 0.500 1.000 92.954 108.526 REMARK  1_bss: 1.1624e+01 1.9406e−01 0.500 1.000  92.954 108.526 REMARK  1_xyz: 1.1498e+01 1.7959e−01 0.500 1.000  92.865 109.494 REMARK  1_adp: 1.1498e+01 1.7959e−01 0.500 1.000  92.865 109.494 REMARK  2_bss: 1.1498e+01 1.7959e−01 0.500 1.000  92.865 109.494 REMARK  2_xyz: 3.6207e+00 1.8788e−01 0.500 1.000 149.180 154.067 REMARK  2_sar: 3.6207e+00 1.8788e−01 0.500 1.000 149.180 154.067 REMARK  2_xyz: 3.6207e+00 1.8788e−01 0.500 1.000 149.180 154.067 REMARK  2_adp: 3.6207e+00 1.8788e−01 0.500 1.000 149.180 154.067 REMARK  3_bss: 3.6207e+00 1.8788e−01 0.500 1.000 149.180 154.067 REMARK  3_xyz: 3.1559e+00 1.8905e−01 0.500 1.000 165.525 158.557 REMARK  3_adp: 3.1559e+00 1.8905e−01 0.500 1.000 165.525 158.557 REMARK  3_bss: 3.1559e+00 1.8905e−01 0.500 1.000 165.525 158.557 REMARK ------------------------------------------------------------- REMARK stage k_sol b_sol b11 b22 b33 b12 b13 b23 REMARK  0 : 0.000 0.000 0.000 0.000 0.000 0.000 0.000 0.000 REMARK  1_bss: 0.336 44.351 −4.572  9.380 −4.076 0.798 0.420 −2.128 REMARK  1_xyz: 0.336 44.351 −4.572  9.380 −4.076 0.798 0.420 −2.128 REMARK  1_adp: 0.336 44.351 −4.572  9.380 −4.076 0.798 0.420 −2.128 REMARK  2_bss: 0.337 44.351 −3.446 10.002 −2.498 0.680 0.454 −2.138 REMARK  2_xyz: 0.337 44.351 −3.446 10.002 −2.498 0.680 0.454 −2.138 REMARK  2_sar: 0.337 44.351 −3.446 10.002 −2.498 0.680 0.454 −2.138 REMARK  2_xyz: 0.337 44.351 −3.446 10.002 −2.498 0.680 0.454 −2.138 REMARK  2_adp: 0.337 44.351 −3.446 10.002 −2.498 0.680 0.454 −2.138 REMARK  3_bss: 0.337 44.484 −2.739 10.984 −1.520 0.618 0.478 −2.262 REMARK  3_xyz: 0.337 44.484 −2.739 10.984 −1.520 0.618 0.478 −2.262 REMARK  3_adp: 0.337 44.484 −2.739 10.984 −1.520 0.618 0.478 −2.262 REMARK  3_bss: 0.338 47.639 −5.103  8.843 −3.740 0.599 0.483 −2.334 REMARK ------------------------------------------------------------- REMARK stage <pher> fom alpha  beta REMARK  0 : 32.034 0.7531 0.3593 3972.999 REMARK  1_bss: 28.896 0.7883 0.3815 2730.148 REMARK  1_xyz: 29.216 0.7842 0.3789 2776.956 REMARK  1_adp: 28.686 0.7901 0.3715 2711.543 REMARK  2_bss: 28.395 0.7932 0.3811 2630.430 REMARK  2_xyz: 28.204 0.7957 0.3830 2624.650 REMARK  2_sar: 28.178 0.7960 0.3831 2632.925 REMARK  2_xyz: 28.195 0.7958 0.3831 2633.352 REMARK  2_adp: 28.130 0.7966 0.3761 2630.693 REMARK  3_bss: 28.127 0.7966 0.3826 2628.991 REMARK  3_xyz: 28.065 0.7974 0.3830 2627.379 REMARK  3_adp: 28.043 0.7976 0.3764 2627.304 REMARK  3_bss: 28.046 0.7976 0.3831 2626.244 REMARK ------------------------------------------------------------- REMARK stage  angl bond chir dihe plan repu geom_target wc REMARK  0 : 2.000 0.025 0.090 25.199 0.019 4.533 2.8592e+04 1.00 REMARK  1_bss: 2.000 0.025 0.090 25.199 0.019 4.533 2.8592e+04 1.00 REMARK  1_xyz: 2.184 0.024 0.124 25.897 0.009 4.315 2.7383e+04 1.00 REMARK  1_adp: 2.184 0.024 0.124 25.897 0.009 4.315 2.7383e+04 1.00 REMARK  2_bss: 2.184 0.024 0.124 25.897 0.009 4.315 2.7383e+04 1.00 REMARK  2_xyz: 1.285 0.012 0.079 25.338 0.005 4.317 1.2130e+04 1.00 REMARK  2_sar: 1.478 0.014 0.088 25.417 0.006 4.315 1.5055e+04 1.00 REMARK  2_xyz: 1.287 0.012 0.080 25.206 0.005 4.315 1.2018e+04 1.00 REMARK  2_adp: 1.287 0.012 0.080 25.206 0.005 4.315 1.2018e+04 1.00 REMARK  3_bss: 1.287 0.012 0.080 25.206 0.005 4.315 1.2018e+04 1.00 REMARK  3_xyz: 1.183 0.011 0.075 25.170 0.005 4.315 1.0760e+04 1.00 REMARK  3_adp: 1.183 0.011 0.075 25.170 0.005 4.315 1.0760e+04 1.00 REMARK  3_bss: 1.183 0.011 0.075 25.170 0.005 4.315 1.0760e+04 1.00 REMARK ------------------------------------------------------------- REMARK      Maximal deviations: REMARK stage  angl bond chir dihe plan repu  |grad| REMARK  0 :70.460 0.820 0.413 174.976 0.340 1.491 2.4900e−01 REMARK  1_bss: 70.460 0.820 0.413 174.976 0.340 1.491 2.4900e−01 REMARK  1_xyz: 18.309 0.587 0.511 173.972 0.079 2.063 8.4482e−02 REMARK  1_adp: 18.309 0.587 0.511 173.972 0.079 2.063 8.4482e−02 REMARK  2_bss: 18.309 0.587 0.511 173.972 0.079 2.063 8.4482e−02 REMARK  2_xyz: 11.636 0.470 0.373 173.016 0.048 2.240 3.1598e−02 REMARK  2_sar: 11.173 0.375 0.450 174.183 0.045 2.143 6.2998e−02 REMARK  2_xyz: 11.532 0.445 0.387 169.382 0.048 2.206 3.1147e−02 REMARK  2_adp: 11.532 0.445 0.387 169.382 0.048 2.206 3.1147e−02 REMARK  3_bss: 11.532 0.445 0.387 169.382 0.048 2.206 3.1147e−02 REMARK  3_xyz: 11.356 0.380 0.374 170.893 0.048 2.231 3.1049e−02 REMARK  3_adp: 11.356 0.380 0.374 170.893 0.048 2.231 3.1049e−02 REMARK  3_bss: 11.356 0.380 0.374 170.893 0.048 2.231 3.1049e−02 REMARK ------------------------------------------------------------- REMARK    |-----overall-----|---macromolecule----|------solvent------| REMARK stage b_max b_min b_ave b_max b_min b_ave b_max b_min b_ave REMARK  0 :170.05 10.55 46.37 170.05 10.55 46.39 40.00 40.00 40.00 REMARK  1_bss: 170.05 10.55 46.37 170.05 10.55 46.39 40.00 40.00 40.00 REMARK  1_xyz: 170.05 10.55 46.37 170.05 10.55 46.39 40.00 40.00 40.00 REMARK  1_adp: 157.99  9.40 44.98 157.99  9.40 45.01 57.42 16.23 33.87 REMARK  2_bss: 157.99  9.40 44.98 157.99  9.40 45.01 57.42 16.23 33.87 REMARK  2_xyz: 157.99  9.40 44.98 157.99  9.40 45.01 57.42 16.23 33.87 REMARK  2_sar: 157.99  9.40 44.98 157.99  9.40 45.01 57.42 16.23 33.87 REMARK  2_xyz: 157.99  9.40 44.98 157.99  9.40 45.01 57.42 16.23 33.87 REMARK  2_adp: 159.29  8.52 44.14 159.29  8.52 44.18 58.11 11.66 31.36 REMARK  3_bss: 159.29  8.52 44.14 159.29  8.52 44.18 58.11 11.66 31.36 REMARK  3_xyz: 159.29  8.52 44.14 159.29  8.52 44.18 58.11 11.66 31.36 REMARK  3_adp: 159.34  8.14 43.37 159.34  8.14 43.41 57.78 10.40 30.30 REMARK  3_bss: 162.50 11.29 46.52 162.50 11.29 46.56 60.94 13.55 33.46 REMARK ------------------------------------------------------------- REMARK stage   Deviation of refined REMARK    model from start model REMARK     max min mean REMARK  0 : 0.000 0.000 0.000 REMARK  1_bss: 0.000 0.000 0.000 REMARK  1_xyz: 2.097 0.006 0.133 REMARK  1_adp: 2.097 0.006 0.133 REMARK  2_bss: 2.097 0.006 0.133 REMARK  2_xyz: 2.036 0.004 0.132 REMARK  2_sar: 2.083 0.006 0.141 REMARK  2_xyz: 2.186 0.003 0.142 REMARK  2_adp: 2.186 0.003 0.142 REMARK  3_bss: 2.186 0.003 0.142 REMARK  3_xyz: 2.221 0.002 0.145 REMARK  3_adp: 2.221 0.002 0.145 REMARK  3_bss: 2.221 0.002 0.145 REMARK ------------------------------------------------------------- REMARK stage   k1_w k1_t k3_w k3_t scale_ml REMARK  0 : 0.3208 0.3361 0.3631 0.3758 1.0000 REMARK  1_bss: 0.4368 0.4308 0.4531 0.4522 1.0000 REMARK  1_xyz: 0.4385 0.4303 0.4529 0.4518 1.0000 REMARK  1_adp: 0.4317 0.4227 0.4454 0.4433 1.0000 REMARK  2_bss: 0.4388 0.4305 0.4528 0.4509 1.0000 REMARK  2_xyz: 0.4388 0.4315 0.4535 0.4519 1.0000 REMARK  2_sar: 0.4387 0.4314 0.4535 0.4518 1.0000 REMARK  2_xyz: 0.4390 0.4316 0.4536 0.4521 1.0000 REMARK  2_adp: 0.4332 0.4259 0.4474 0.4460 1.0000 REMARK  3_bss: 0.4384 0.4311 0.4528 0.4515 1.0000 REMARK  3_xyz: 0.4385 0.4314 0.4529 0.4518 1.0000 REMARK  3_adp: 0.4331 0.4258 0.4473 0.4460 1.0000 REMARK  3_bss: 0.4385 0.4313 0.4529 0.4517 1.0000 REMARK ------------------------------------------------------------- REMARK r_free_flags.md5.hexdigest 38c8444a6d884020b443671f38202fe9

TABLE A CRYST1 55.500 86.800 95.500 67.60 73.30 85.80 P 1 SCALE1 0.018018 −0.001323 −0.005298 0.00000 SCALE2 0.000000 0.011552 −0.004700 0.00000 SCALE3 0.000000 0.000000 0.011803 0.00000 ATOM 1 N TRP A 32 5.479 23.414 49.677 1.00 83.99 N ATOM 2 CA TRP A 32 6.029 23.314 48.327 1.00 103.53 C ATOM 3 C TRP A 32 5.622 24.515 47.517 1.00 92.41 C ATOM 4 O TRP A 32 6.122 24.745 46.414 1.00 93.58 O ATOM 5 CB TRP A 32 5.551 22.043 47.616 1.00 107.68 C ATOM 6 CG TRP A 32 6.380 20.867 47.950 1.00 115.39 C ATOM 7 CD1 TRP A 32 7.549 20.491 47.357 1.00 115.64 C ATOM 8 CD2 TRP A 32 6.126 19.916 48.986 1.00 125.36 C ATOM 9 NE1 TRP A 32 8.036 19.356 47.956 1.00 131.84 N ATOM 10 CE2 TRP A 32 7.181 18.983 48.960 1.00 137.20 C ATOM 11 CE3 TRP A 32 5.107 19.761 49.930 1.00 130.64 C ATOM 12 CZ2 TRP A 32 7.243 17.905 49.844 1.00 144.93 C ATOM 13 CZ3 TRP A 32 5.169 18.693 50.806 1.00 138.72 C ATOM 14 CH2 TRP A 32 6.230 17.778 50.757 1.00 143.16 C ATOM 15 N GLU A 33 4.700 25.286 48.066 1.00 75.79 N ATOM 16 CA GLU A 33 4.178 26.417 47.327 1.00 71.94 C ATOM 17 C GLU A 33 5.049 27.654 47.518 1.00 63.78 C ATOM 18 O GLU A 33 5.368 28.347 46.553 1.00 57.27 O ATOM 19 CB GLU A 33 2.739 26.700 47.718 1.00 62.61 C ATOM 20 CG GLU A 33 2.043 27.620 46.749 1.00 80.74 C ATOM 21 CD GLU A 33 0.731 28.138 47.287 1.00 97.56 C ATOM 22 OE1 GLU A 33 0.304 27.692 48.375 1.00 98.25 O ATOM 23 OE2 GLU A 33 0.128 28.998 46.621 1.00 93.05 O ATOM 24 N ALA A 34 5.429 27.931 48.761 1.00 58.96 N ATOM 25 CA ALA A 34 6.443 28.945 49.009 1.00 55.06 C ATOM 26 C ALA A 34 7.704 28.540 48.253 1.00 53.77 C ATOM 27 O ALA A 34 8.300 29.353 47.549 1.00 52.18 O ATOM 28 CB ALA A 34 6.728 29.076 50.492 1.00 34.43 C ATOM 29 N GLY A 35 8.089 27.273 48.390 1.00 47.25 N ATOM 30 CA GLY A 35 9.239 26.738 47.682 1.00 48.47 C ATOM 31 C GLY A 35 9.179 26.934 46.180 1.00 50.10 C ATOM 32 O GLY A 35 10.011 27.627 45.597 1.00 43.83 O ATOM 33 N MET A 36 8.184 26.333 45.541 1.00 58.69 N ATOM 34 CA MET A 36 8.045 26.463 44.098 1.00 45.18 C ATOM 35 C MET A 36 8.044 27.925 43.671 1.00 43.86 C ATOM 36 O MET A 36 8.733 28.301 42.723 1.00 52.46 O ATOM 37 CB MET A 36 6.803 25.724 43.597 1.00 50.39 C ATOM 38 CG MET A 36 6.911 24.197 43.705 1.00 65.16 C ATOM 39 SD MET A 36 8.354 23.460 42.883 1.00 75.80 S ATOM 40 CE MET A 36 9.662 23.650 44.107 1.00 53.23 C ATOM 41 N SER A 37 7.292 28.754 44.384 1.00 41.05 N ATOM 42 CA SER A 37 7.224 30.183 44.073 1.00 42.61 C ATOM 43 C SER A 37 8.597 30.850 44.051 1.00 39.66 C ATOM 44 O SER A 37 8.904 31.646 43.162 1.00 27.74 O ATOM 45 CB SER A 37 6.320 30.910 45.071 1.00 43.91 C ATOM 46 OG SER A 37 4.961 30.572 44.865 1.00 49.57 O ATOM 47 N LEU A 38 9.420 30.534 45.043 1.00 37.24 N ATOM 48 CA LEU A 38 10.745 31.125 45.115 1.00 42.45 C ATOM 49 C LEU A 38 11.632 30.645 43.953 1.00 44.56 C ATOM 50 O LEU A 38 12.216 31.458 43.225 1.00 36.02 O ATOM 51 CB LEU A 38 11.394 30.835 46.467 1.00 35.05 C ATOM 52 CG LEU A 38 12.715 31.573 46.694 1.00 43.51 C ATOM 53 CD1 LEU A 38 12.507 33.088 46.715 1.00 34.04 C ATOM 54 CD2 LEU A 38 13.369 31.098 47.974 1.00 36.94 C ATOM 55 N LEU A 39 11.716 29.329 43.774 1.00 37.17 N ATOM 56 CA LEU A 39 12.446 28.768 42.643 1.00 42.97 C ATOM 57 C LEU A 39 12.100 29.478 41.323 1.00 41.17 C ATOM 58 O LEU A 39 12.989 29.831 40.547 1.00 38.80 O ATOM 59 CB LEU A 39 12.195 27.263 42.518 1.00 42.81 C ATOM 60 CG LEU A 39 12.958 26.578 41.380 1.00 42.86 C ATOM 61 CD1 LEU A 39 14.458 26.501 41.687 1.00 38.86 C ATOM 62 CD2 LEU A 39 12.381 25.194 41.098 1.00 49.27 C ATOM 63 N MET A 40 10.810 29.692 41.076 1.00 37.62 N ATOM 64 CA MET A 40 10.368 30.354 39.843 1.00 33.30 C ATOM 65 C MET A 40 10.811 31.822 39.739 1.00 35.57 C ATOM 66 O MET A 40 11.224 32.277 38.678 1.00 29.74 O ATOM 67 CB MET A 40 8.850 30.223 39.667 1.00 38.00 C ATOM 68 CG MET A 40 8.360 28.785 39.457 1.00 57.02 C ATOM 69 SD MET A 40 9.045 27.919 38.005 1.00 83.10 S ATOM 70 CE MET A 40 10.548 27.189 38.673 1.00 47.31 C ATOM 71 N ALA A 41 10.740 32.564 40.839 1.00 42.39 N ATOM 72 CA ALA A 41 11.243 33.931 40.838 1.00 32.14 C ATOM 73 C ALA A 41 12.771 33.936 40.715 1.00 37.71 C ATOM 74 O ALA A 41 13.378 34.983 40.503 1.00 34.34 O ATOM 75 CB ALA A 41 10.814 34.647 42.102 1.00 38.26 C ATOM 76 N LEU A 42 13.379 32.758 40.835 1.00 32.06 N ATOM 77 CA LEU A 42 14.835 32.630 40.852 1.00 38.43 C ATOM 78 C LEU A 42 15.479 31.951 39.621 1.00 37.50 C ATOM 79 O LEU A 42 16.701 32.057 39.448 1.00 33.31 O ATOM 80 CB LEU A 42 15.284 31.911 42.142 1.00 42.24 C ATOM 81 CG LEU A 42 16.054 32.627 43.266 1.00 30.07 C ATOM 82 CD1 LEU A 42 15.917 34.119 43.213 1.00 27.33 C ATOM 83 CD2 LEU A 42 15.628 32.124 44.613 1.00 23.94 C ATOM 84 N VAL A 43 14.685 31.268 38.779 1.00 30.39 N ATOM 85 CA VAL A 43 15.249 30.423 37.688 1.00 31.64 C ATOM 86 C VAL A 43 16.172 31.090 36.674 1.00 30.23 C ATOM 87 O VAL A 43 17.251 30.580 36.414 1.00 34.48 O ATOM 88 CB VAL A 43 14.196 29.668 36.847 1.00 28.23 C ATOM 89 CG1 VAL A 43 14.255 28.170 37.121 1.00 31.36 C ATOM 90 CG2 VAL A 43 12.806 30.254 37.029 1.00 43.70 C ATOM 91 N VAL A 44 15.735 32.183 36.058 1.00 25.45 N ATOM 92 CA VAL A 44 16.586 32.861 35.093 1.00 25.39 C ATOM 93 C VAL A 44 17.953 33.133 35.693 1.00 31.88 C ATOM 94 O VAL A 44 18.972 32.858 35.063 1.00 36.72 O ATOM 95 CB VAL A 44 15.980 34.173 34.582 1.00 33.02 C ATOM 96 CG1 VAL A 44 16.977 34.908 33.706 1.00 20.74 C ATOM 97 CG2 VAL A 44 14.697 33.896 33.819 1.00 29.01 C ATOM 98 N LEU A 45 17.972 33.649 36.919 1.00 34.27 N ATOM 99 CA LEU A 45 19.226 33.872 37.631 1.00 34.28 C ATOM 100 C LEU A 45 19.967 32.552 37.856 1.00 33.96 C ATOM 101 O LEU A 45 21.116 32.404 37.434 1.00 35.46 O ATOM 102 CB LEU A 45 18.991 34.589 38.962 1.00 25.07 C ATOM 103 CG LEU A 45 20.249 34.728 39.828 1.00 35.24 C ATOM 104 CD1 LEU A 45 21.202 35.825 39.313 1.00 24.13 C ATOM 105 CD2 LEU A 45 19.870 34.972 41.275 1.00 34.92 C ATOM 106 N LEU A 46 19.299 31.600 38.505 1.00 29.50 N ATOM 107 CA LEU A 46 19.877 30.279 38.797 1.00 34.70 C ATOM 108 C LEU A 46 20.472 29.516 37.598 1.00 36.81 C ATOM 109 O LEU A 46 21.490 28.835 37.730 1.00 39.64 O ATOM 110 CB LEU A 46 18.841 29.386 39.479 1.00 33.97 C ATOM 111 CG LEU A 46 18.535 29.691 40.938 1.00 37.67 C ATOM 112 CD1 LEU A 46 17.621 28.615 41.508 1.00 38.94 C ATOM 113 CD2 LEU A 46 19.832 29.762 41.698 1.00 28.47 C ATOM 114 N ILE A 47 19.821 29.606 36.443 1.00 33.68 N ATOM 115 CA ILE A 47 20.318 28.953 35.236 1.00 37.11 C ATOM 116 C ILE A 47 21.516 29.703 34.651 1.00 35.09 C ATOM 117 O ILE A 47 22.527 29.088 34.333 1.00 31.56 O ATOM 118 CB ILE A 47 19.215 28.815 34.144 1.00 34.69 C ATOM 119 CG1 ILE A 47 18.103 27.868 34.593 1.00 33.71 C ATOM 120 CG2 ILE A 47 19.804 28.309 32.857 1.00 26.83 C ATOM 121 CD1 ILE A 47 16.810 27.998 33.786 1.00 24.38 C ATOM 122 N VAL A 48 21.395 31.026 34.518 1.00 36.00 N ATOM 123 CA VAL A 48 22.413 31.842 33.857 1.00 29.90 C ATOM 124 C VAL A 48 23.676 32.035 34.684 1.00 33.15 C ATOM 125 O VAL A 48 24.773 31.740 34.214 1.00 41.11 O ATOM 126 CB VAL A 48 21.877 33.226 33.428 1.00 29.31 C ATOM 127 CG1 VAL A 48 23.017 34.123 32.978 1.00 21.44 C ATOM 128 CG2 VAL A 48 20.864 33.080 32.317 1.00 29.53 C ATOM 129 N ALA A 49 23.533 32.542 35.902 1.00 33.37 N ATOM 130 CA ALA A 49 24.692 32.758 36.768 1.00 38.03 C ATOM 131 C ALA A 49 25.399 31.441 37.089 1.00 40.97 C ATOM 132 O ALA A 49 26.626 31.388 37.164 1.00 37.86 O ATOM 133 CB ALA A 49 24.278 33.457 38.047 1.00 30.38 C ATOM 134 N GLY A 50 24.614 30.383 37.277 1.00 40.04 N ATOM 135 CA GLY A 50 25.143 29.083 37.650 1.00 33.14 C ATOM 136 C GLY A 50 25.866 28.360 36.524 1.00 40.38 C ATOM 137 O GLY A 50 26.825 27.625 36.758 1.00 40.26 O ATOM 138 N ASN A 51 25.408 28.545 35.292 1.00 31.96 N ATOM 139 CA ASN A 51 26.053 27.877 34.175 1.00 32.47 C ATOM 140 C ASN A 51 27.200 28.705 33.643 1.00 32.88 C ATOM 141 O ASN A 51 28.197 28.165 33.191 1.00 33.20 O ATOM 142 CB ASN A 51 25.051 27.541 33.080 1.00 30.53 C ATOM 143 CG ASN A 51 24.223 26.313 33.417 1.00 37.29 C ATOM 144 OD1 ASN A 51 24.649 25.173 33.188 1.00 28.91 O ATOM 145 ND2 ASN A 51 23.026 26.540 33.963 1.00 28.81 N ATOM 146 N VAL A 52 27.055 30.023 33.706 1.00 33.30 N ATOM 147 CA VAL A 52 28.163 30.912 33.423 1.00 30.80 C ATOM 148 C VAL A 52 29.286 30.565 34.390 1.00 43.40 C ATOM 149 O VAL A 52 30.469 30.618 34.045 1.00 35.89 O ATOM 150 CB VAL A 52 27.779 32.377 33.614 1.00 30.90 C ATOM 151 CG1 VAL A 52 29.020 33.215 33.845 1.00 20.60 C ATOM 152 CG2 VAL A 52 27.002 32.884 32.406 1.00 33.55 C ATOM 153 N LEU A 53 28.901 30.175 35.600 1.00 42.58 N ATOM 154 CA LEU A 53 29.864 29.853 36.642 1.00 39.51 C ATOM 155 C LEU A 53 30.575 28.520 36.399 1.00 44.56 C ATOM 156 O LEU A 53 31.778 28.407 36.628 1.00 42.77 O ATOM 157 CB LEU A 53 29.175 29.850 38.001 1.00 40.87 C ATOM 158 CG LEU A 53 29.978 30.484 39.139 1.00 71.27 C ATOM 159 CD1 LEU A 53 30.315 31.943 38.829 1.00 53.98 C ATOM 160 CD2 LEU A 53 29.205 30.373 40.440 1.00 80.71 C ATOM 161 N VAL A 54 29.831 27.514 35.940 1.00 45.68 N ATOM 162 CA VAL A 54 30.419 26.222 35.584 1.00 40.52 C ATOM 163 C VAL A 54 31.416 26.409 34.441 1.00 42.52 C ATOM 164 O VAL A 54 32.523 25.873 34.458 1.00 40.69 O ATOM 165 CB VAL A 54 29.338 25.203 35.145 1.00 40.15 C ATOM 166 CG1 VAL A 54 29.970 24.032 34.394 1.00 32.03 C ATOM 167 CG2 VAL A 54 28.533 24.712 36.337 1.00 33.68 C ATOM 168 N ILE A 55 31.009 27.181 33.444 1.00 39.95 N ATOM 169 CA ILE A 55 31.864 27.461 32.306 1.00 44.35 C ATOM 170 C ILE A 55 33.167 28.125 32.762 1.00 51.31 C ATOM 171 O ILE A 55 34.245 27.759 32.306 1.00 60.77 O ATOM 172 CB ILE A 55 31.124 28.318 31.249 1.00 36.78 C ATOM 173 CG1 ILE A 55 30.298 27.421 30.324 1.00 30.86 C ATOM 174 CG2 ILE A 55 32.092 29.161 30.447 1.00 23.46 C ATOM 175 CD1 ILE A 55 29.288 28.185 29.492 1.00 32.30 C ATOM 176 N ALA A 56 33.073 29.079 33.680 1.00 44.33 N ATOM 177 CA ALA A 56 34.260 29.803 34.109 1.00 40.24 C ATOM 178 C ALA A 56 35.166 28.941 34.985 1.00 44.67 C ATOM 179 O ALA A 56 36.382 29.020 34.887 1.00 56.47 O ATOM 180 CB ALA A 56 33.879 31.093 34.825 1.00 41.62 C ATOM 181 N ALA A 57 34.576 28.122 35.845 1.00 41.10 N ATOM 182 CA ALA A 57 35.360 27.233 36.692 1.00 46.52 C ATOM 183 C ALA A 57 36.164 26.255 35.842 1.00 51.89 C ATOM 184 O ALA A 57 37.365 26.086 36.036 1.00 56.20 O ATOM 185 CB ALA A 57 34.456 26.475 37.664 1.00 38.14 C ATOM 186 N ILE A 58 35.489 25.609 34.898 1.00 50.72 N ATOM 187 CA ILE A 58 36.141 24.662 34.007 1.00 55.77 C ATOM 188 C ILE A 58 37.234 25.356 33.203 1.00 52.34 C ATOM 189 O ILE A 58 38.212 24.732 32.800 1.00 69.28 O ATOM 190 CB ILE A 58 35.126 24.000 33.045 1.00 50.04 C ATOM 191 CG1 ILE A 58 34.268 22.972 33.787 1.00 41.61 C ATOM 192 CG2 ILE A 58 35.833 23.333 31.881 1.00 44.93 C ATOM 193 CD1 ILE A 58 33.148 22.407 32.941 1.00 29.39 C ATOM 194 N GLY A 59 37.069 26.654 32.983 1.00 47.92 N ATOM 195 CA GLY A 59 38.017 27.423 32.197 1.00 54.58 C ATOM 196 C GLY A 59 39.134 28.073 33.000 1.00 57.00 C ATOM 197 O GLY A 59 40.032 28.681 32.432 1.00 57.28 O ATOM 198 N SER A 60 39.079 27.956 34.321 1.00 52.25 N ATOM 199 CA SER A 60 40.149 28.459 35.171 1.00 52.71 C ATOM 200 C SER A 60 41.058 27.304 35.543 1.00 68.82 C ATOM 201 O SER A 60 42.132 27.132 34.964 1.00 90.28 O ATOM 202 CB SER A 60 39.589 29.097 36.447 1.00 65.02 C ATOM 203 OG SER A 60 39.016 30.368 36.193 1.00 65.89 O ATOM 204 N THR A 61 40.613 26.512 36.514 1.00 67.59 N ATOM 205 CA THR A 61 41.335 25.325 36.955 1.00 71.80 C ATOM 206 C THR A 61 41.599 24.378 35.797 1.00 82.94 C ATOM 207 O THR A 61 40.694 23.663 35.364 1.00 82.55 O ATOM 208 CB THR A 61 40.516 24.522 37.976 1.00 64.49 C ATOM 209 OG1 THR A 61 39.657 25.398 38.712 1.00 65.85 O ATOM 210 CG2 THR A 61 41.438 23.769 38.923 1.00 79.54 C ATOM 211 N GLN A 62 42.833 24.364 35.301 1.00 92.97 N ATOM 212 CA GLN A 62 43.225 23.405 34.273 1.00 99.18 C ATOM 213 C GLN A 62 43.106 21.999 34.853 1.00 95.18 C ATOM 214 O GLN A 62 42.926 21.016 34.124 1.00 88.85 O ATOM 215 CB GLN A 62 44.648 23.696 33.797 1.00 107.65 C ATOM 216 CG GLN A 62 44.767 25.037 33.086 1.00 118.47 C ATOM 217 CD GLN A 62 46.074 25.741 33.371 1.00 138.62 C ATOM 218 OE1 GLN A 62 47.106 25.102 33.583 1.00 149.46 O ATOM 219 NE2 GLN A 62 46.037 27.071 33.382 1.00 136.58 N ATOM 220 N ARG A 63 43.192 21.933 36.179 1.00 73.75 N ATOM 221 CA ARG A 63 42.943 20.720 36.940 1.00 67.13 C ATOM 222 C ARG A 63 41.479 20.264 36.808 1.00 80.88 C ATOM 223 O ARG A 63 41.130 19.135 37.158 1.00 78.75 O ATOM 224 CB ARG A 63 43.288 20.986 38.400 1.00 85.45 C ATOM 225 CG ARG A 63 42.782 19.954 39.377 1.00 97.30 C ATOM 226 CD ARG A 63 42.420 20.622 40.683 1.00 103.16 C ATOM 227 NE ARG A 63 42.561 19.729 41.827 1.00 120.92 N ATOM 228 CZ ARG A 63 42.028 19.966 43.022 1.00 126.50 C ATOM 229 NH1 ARG A 63 41.305 21.064 43.220 1.00 114.21 N ATOM 230 NH2 ARG A 63 42.208 19.104 44.015 1.00 122.66 N ATOM 231 N LEU A 64 40.624 21.158 36.316 1.00 81.30 N ATOM 232 CA LEU A 64 39.252 20.813 35.948 1.00 64.33 C ATOM 233 C LEU A 64 39.121 20.686 34.430 1.00 68.67 C ATOM 234 O LEU A 64 38.023 20.521 33.907 1.00 58.81 O ATOM 235 CB LEU A 64 38.269 21.874 36.439 1.00 62.31 C ATOM 236 CG LEU A 64 37.609 21.730 37.812 1.00 61.10 C ATOM 237 CD1 LEU A 64 36.568 22.830 37.993 1.00 51.33 C ATOM 238 CD2 LEU A 64 36.987 20.355 37.998 1.00 42.50 C ATOM 239 N GLN A 65 40.239 20.779 33.718 1.00 73.78 N ATOM 240 CA GLN A 65 40.206 20.632 32.269 1.00 81.50 C ATOM 241 C GLN A 65 40.478 19.193 31.841 1.00 74.21 C ATOM 242 O GLN A 65 41.621 18.739 31.814 1.00 69.96 O ATOM 243 CB GLN A 65 41.149 21.625 31.586 1.00 76.94 C ATOM 244 CG GLN A 65 40.470 22.945 31.258 1.00 77.65 C ATOM 245 CD GLN A 65 41.430 23.980 30.721 1.00 98.72 C ATOM 246 OE1 GLN A 65 42.560 24.091 31.193 1.00 98.33 O ATOM 247 NE2 GLN A 65 40.983 24.752 29.731 1.00 96.05 N ATOM 248 N THR A 66 39.398 18.482 31.529 1.00 63.49 N ATOM 249 CA THR A 66 39.456 17.080 31.150 1.00 51.39 C ATOM 250 C THR A 66 38.438 16.838 30.041 1.00 44.86 C ATOM 251 O THR A 66 37.529 17.639 29.856 1.00 44.94 O ATOM 252 CB THR A 66 39.151 16.162 32.361 1.00 52.62 C ATOM 253 OG1 THR A 66 37.787 16.325 32.773 1.00 45.47 O ATOM 254 CG2 THR A 66 40.053 16.508 33.529 1.00 46.17 C ATOM 255 N LEU A 67 38.601 15.750 29.295 1.00 46.24 N ATOM 256 CA LEU A 67 37.660 15.390 28.238 1.00 42.57 C ATOM 257 C LEU A 67 36.206 15.476 28.693 1.00 47.62 C ATOM 258 O LEU A 67 35.410 16.219 28.116 1.00 40.50 O ATOM 259 CB LEU A 67 37.936 13.971 27.746 1.00 55.94 C ATOM 260 CG LEU A 67 39.184 13.828 26.886 1.00 47.72 C ATOM 261 CD1 LEU A 67 39.151 12.502 26.157 1.00 62.62 C ATOM 262 CD2 LEU A 67 39.241 14.978 25.910 1.00 43.96 C ATOM 263 N THR A 68 35.864 14.701 29.721 1.00 36.53 N ATOM 264 CA THR A 68 34.515 14.707 30.266 1.00 40.04 C ATOM 265 C THR A 68 33.985 16.134 30.490 1.00 35.56 C ATOM 266 O THR A 68 32.825 16.420 30.204 1.00 42.74 O ATOM 267 CB THR A 68 34.415 13.870 31.573 1.00 36.84 C ATOM 268 OG1 THR A 68 34.619 12.485 31.279 1.00 36.37 O ATOM 269 CG2 THR A 68 33.051 14.018 32.205 1.00 37.20 C ATOM 270 N ASN A 69 34.835 17.032 30.973 1.00 34.20 N ATOM 271 CA ASN A 69 34.406 18.402 31.285 1.00 35.19 C ATOM 272 C ASN A 69 34.169 19.306 30.074 1.00 34.58 C ATOM 273 O ASN A 69 33.473 20.315 30.179 1.00 31.28 O ATOM 274 CB ASN A 69 35.366 19.066 32.276 1.00 35.89 C ATOM 275 CG ASN A 69 35.169 18.564 33.690 1.00 53.27 C ATOM 276 OD1 ASN A 69 34.115 18.010 34.014 1.00 48.94 O ATOM 277 ND2 ASN A 69 36.179 18.742 34.542 1.00 58.63 N ATOM 278 N LEU A 70 34.752 18.946 28.933 1.00 34.78 N ATOM 279 CA LEU A 70 34.447 19.612 27.674 1.00 31.35 C ATOM 280 C LEU A 70 32.981 19.354 27.300 1.00 33.12 C ATOM 281 O LEU A 70 32.251 20.263 26.900 1.00 26.98 O ATOM 282 CB LEU A 70 35.370 19.100 26.574 1.00 38.11 C ATOM 283 CG LEU A 70 36.710 19.804 26.387 1.00 34.46 C ATOM 284 CD1 LEU A 70 37.517 19.192 25.216 1.00 30.63 C ATOM 285 CD2 LEU A 70 36.437 21.273 26.155 1.00 37.05 C ATOM 286 N PHE A 71 32.556 18.106 27.444 1.00 27.08 N ATOM 287 CA PHE A 71 31.167 17.749 27.248 1.00 29.77 C ATOM 288 C PHE A 71 30.261 18.483 28.229 1.00 34.66 C ATOM 289 O PHE A 71 29.180 18.945 27.854 1.00 36.20 O ATOM 290 CB PHE A 71 30.979 16.244 27.396 1.00 36.47 C ATOM 291 CG PHE A 71 31.766 15.439 26.402 1.00 41.69 C ATOM 292 CD1 PHE A 71 32.001 15.933 25.131 1.00 33.87 C ATOM 293 CD2 PHE A 71 32.261 14.184 26.732 1.00 39.10 C ATOM 294 CE1 PHE A 71 32.717 15.194 24.215 1.00 35.55 C ATOM 295 CE2 PHE A 71 32.981 13.448 25.815 1.00 35.39 C ATOM 296 CZ PHE A 71 33.211 13.953 24.559 1.00 28.51 C ATOM 297 N ILE A 72 30.700 18.583 29.482 1.00 31.33 N ATOM 298 CA ILE A 72 29.966 19.322 30.509 1.00 28.07 C ATOM 299 C ILE A 72 29.721 20.765 30.064 1.00 29.37 C ATOM 300 O ILE A 72 28.672 21.346 30.328 1.00 33.16 O ATOM 301 CB ILE A 72 30.729 19.320 31.845 1.00 32.56 C ATOM 302 CG1 ILE A 72 30.720 17.924 32.472 1.00 30.68 C ATOM 303 CG2 ILE A 72 30.155 20.350 32.806 1.00 32.38 C ATOM 304 CD1 ILE A 72 29.363 17.339 32.658 1.00 23.38 C ATOM 305 N THR A 73 30.702 21.327 29.375 1.00 29.77 N ATOM 306 CA THR A 73 30.635 22.697 28.891 1.00 34.60 C ATOM 307 C THR A 73 29.638 22.856 27.758 1.00 35.71 C ATOM 308 O THR A 73 29.046 23.923 27.584 1.00 40.54 O ATOM 309 CB THR A 73 32.014 23.171 28.394 1.00 27.39 C ATOM 310 OG1 THR A 73 32.973 22.984 29.435 1.00 25.98 O ATOM 311 CG2 THR A 73 31.975 24.648 27.998 1.00 17.40 C ATOM 312 N SER A 74 29.486 21.803 26.964 1.00 32.75 N ATOM 313 CA SER A 74 28.515 21.799 25.882 1.00 32.03 C ATOM 314 C SER A 74 27.156 21.812 26.559 1.00 34.14 C ATOM 315 O SER A 74 26.260 22.585 26.198 1.00 31.27 O ATOM 316 CB SER A 74 28.693 20.540 25.025 1.00 31.36 C ATOM 317 OG SER A 74 27.742 20.462 23.978 1.00 38.64 O ATOM 318 N LEU A 75 27.039 20.960 27.574 1.00 30.55 N ATOM 319 CA LEU A 75 25.827 20.814 28.368 1.00 26.60 C ATOM 320 C LEU A 75 25.392 22.121 29.012 1.00 26.46 C ATOM 321 O LEU A 75 24.198 22.390 29.129 1.00 28.93 O ATOM 322 CB LEU A 75 26.047 19.766 29.446 1.00 24.73 C ATOM 323 CG LEU A 75 24.782 19.050 29.891 1.00 27.34 C ATOM 324 CD1 LEU A 75 23.774 19.026 28.757 1.00 20.89 C ATOM 325 CD2 LEU A 75 25.132 17.642 30.357 1.00 27.17 C ATOM 326 N ALA A 76 26.368 22.926 29.421 1.00 25.85 N ATOM 327 CA ALA A 76 26.113 24.209 30.066 1.00 26.99 C ATOM 328 C ALA A 76 25.709 25.314 29.081 1.00 28.89 C ATOM 329 O ALA A 76 25.024 26.269 29.453 1.00 30.30 O ATOM 330 CB ALA A 76 27.313 24.634 30.881 1.00 23.85 C ATOM 331 N CYS A 77 26.130 25.189 27.828 1.00 29.63 N ATOM 332 CA CYS A 77 25.719 26.144 26.809 1.00 32.36 C ATOM 333 C CYS A 77 24.271 25.895 26.385 1.00 32.08 C ATOM 334 O CYS A 77 23.494 26.836 26.199 1.00 27.57 O ATOM 335 CB CYS A 77 26.659 26.092 25.614 1.00 25.58 C ATOM 336 SG CYS A 77 28.277 26.736 26.014 1.00 43.24 S ATOM 337 N ALA A 78 23.908 24.626 26.236 1.00 30.96 N ATOM 338 CA ALA A 78 22.511 24.273 26.041 1.00 28.35 C ATOM 339 C ALA A 78 21.709 24.998 27.103 1.00 30.79 C ATOM 340 O ALA A 78 20.660 25.566 26.822 1.00 30.86 O ATOM 341 CB ALA A 78 22.309 22.779 26.170 1.00 19.75 C ATOM 342 N ASP A 79 22.233 24.996 28.327 1.00 32.81 N ATOM 343 CA ASP A 79 21.539 25.577 29.475 1.00 27.05 C ATOM 344 C ASP A 79 21.579 27.094 29.477 1.00 26.73 C ATOM 345 O ASP A 79 20.596 27.745 29.817 1.00 26.51 O ATOM 346 CB ASP A 79 22.100 25.022 30.774 1.00 23.51 C ATOM 347 CG ASP A 79 21.485 23.686 31.147 1.00 34.58 C ATOM 348 OD1 ASP A 79 20.690 23.150 30.349 1.00 36.21 O ATOM 349 OD2 ASP A 79 21.799 23.167 32.245 1.00 56.57 O ATOM 350 N LEU A 80 22.708 27.661 29.079 1.00 28.45 N ATOM 351 CA LEU A 80 22.785 29.101 28.908 1.00 33.58 C ATOM 352 C LEU A 80 21.723 29.607 27.912 1.00 37.54 C ATOM 353 O LEU A 80 21.093 30.649 28.110 1.00 32.93 O ATOM 354 CB LEU A 80 24.191 29.499 28.458 1.00 38.99 C ATOM 355 CG LEU A 80 24.665 30.846 29.001 1.00 40.69 C ATOM 356 CD1 LEU A 80 24.238 30.978 30.451 1.00 38.63 C ATOM 357 CD2 LEU A 80 26.169 30.980 28.858 1.00 32.74 C ATOM 358 N VAL A 81 21.515 28.861 26.837 1.00 33.48 N ATOM 359 CA VAL A 81 20.543 29.288 25.847 1.00 38.29 C ATOM 360 C VAL A 81 19.122 29.205 26.404 1.00 32.64 C ATOM 361 O VAL A 81 18.339 30.142 26.253 1.00 36.35 O ATOM 362 CB VAL A 81 20.716 28.530 24.510 1.00 45.83 C ATOM 363 CG1 VAL A 81 19.562 28.832 23.540 1.00 27.22 C ATOM 364 CG2 VAL A 81 22.060 28.905 23.885 1.00 29.91 C ATOM 365 N VAL A 82 18.799 28.098 27.065 1.00 31.63 N ATOM 366 CA VAL A 82 17.507 27.950 27.743 1.00 34.38 C ATOM 367 C VAL A 82 17.228 29.104 28.703 1.00 30.41 C ATOM 368 O VAL A 82 16.094 29.550 28.847 1.00 27.68 O ATOM 369 CB VAL A 82 17.442 26.644 28.546 1.00 28.52 C ATOM 370 CG1 VAL A 82 16.176 26.600 29.389 1.00 22.22 C ATOM 371 CG2 VAL A 82 17.531 25.447 27.615 1.00 26.88 C ATOM 372 N GLY A 83 18.281 29.586 29.350 1.00 34.08 N ATOM 373 CA GLY A 83 18.158 30.628 30.355 1.00 39.88 C ATOM 374 C GLY A 83 18.156 32.061 29.851 1.00 35.32 C ATOM 375 O GLY A 83 17.761 32.965 30.571 1.00 40.85 O ATOM 376 N LEU A 84 18.590 32.282 28.618 1.00 37.86 N ATOM 377 CA LEU A 84 18.672 33.641 28.112 1.00 40.48 C ATOM 378 C LEU A 84 17.612 33.942 27.060 1.00 39.24 C ATOM 379 O LEU A 84 17.124 35.067 26.971 1.00 47.74 O ATOM 380 CB LEU A 84 20.074 33.922 27.567 1.00 40.90 C ATOM 381 CG LEU A 84 21.173 34.013 28.625 1.00 42.58 C ATOM 382 CD1 LEU A 84 22.553 34.077 27.992 1.00 32.38 C ATOM 383 CD2 LEU A 84 20.926 35.226 29.487 1.00 42.05 C ATOM 384 N LEU A 85 17.253 32.941 26.267 1.00 36.07 N ATOM 385 CA LEU A 85 16.299 33.153 25.177 1.00 42.26 C ATOM 386 C LEU A 85 14.961 32.451 25.416 1.00 37.17 C ATOM 387 O LEU A 85 13.910 33.073 25.334 1.00 43.82 O ATOM 388 CB LEU A 85 16.922 32.730 23.847 1.00 38.28 C ATOM 389 CG LEU A 85 18.295 33.386 23.659 1.00 38.79 C ATOM 390 CD1 LEU A 85 19.002 32.817 22.469 1.00 28.13 C ATOM 391 CD2 LEU A 85 18.168 34.904 23.534 1.00 36.04 C ATOM 392 N VAL A 86 15.008 31.166 25.745 1.00 33.87 N ATOM 393 CA VAL A 86 13.799 30.369 25.902 1.00 27.63 C ATOM 394 C VAL A 86 12.941 30.804 27.104 1.00 28.87 C ATOM 395 O VAL A 86 11.818 31.272 26.951 1.00 25.77 O ATOM 396 CB VAL A 86 14.147 28.864 26.035 1.00 24.34 C ATOM 397 CG1 VAL A 86 12.893 28.033 26.259 1.00 19.71 C ATOM 398 CG2 VAL A 86 14.909 28.380 24.815 1.00 19.40 C ATOM 399 N VAL A 87 13.476 30.638 28.305 1.00 34.72 N ATOM 400 CA VAL A 87 12.710 30.895 29.515 1.00 29.78 C ATOM 401 C VAL A 87 12.222 32.348 29.652 1.00 30.68 C ATOM 402 O VAL A 87 11.068 32.581 30.021 1.00 23.47 O ATOM 403 CB VAL A 87 13.485 30.439 30.781 1.00 31.77 C ATOM 404 CG1 VAL A 87 13.050 31.225 31.988 1.00 31.23 C ATOM 405 CG2 VAL A 87 13.269 28.954 31.026 1.00 32.29 C ATOM 406 N PRO A 88 13.095 33.330 29.369 1.00 29.30 N ATOM 407 CA PRO A 88 12.598 34.696 29.523 1.00 28.30 C ATOM 408 C PRO A 88 11.377 34.970 28.659 1.00 27.72 C ATOM 409 O PRO A 88 10.405 35.518 29.167 1.00 37.17 O ATOM 410 CB PRO A 88 13.787 35.554 29.107 1.00 23.80 C ATOM 411 CG PRO A 88 14.957 34.719 29.456 1.00 27.88 C ATOM 412 CD PRO A 88 14.557 33.294 29.210 1.00 31.63 C ATOM 413 N PHE A 89 11.404 34.592 27.389 1.00 33.76 N ATOM 414 CA PHE A 89 10.237 34.824 26.540 1.00 30.21 C ATOM 415 C PHE A 89 9.039 33.964 26.952 1.00 30.78 C ATOM 416 O PHE A 89 7.904 34.434 26.950 1.00 26.22 O ATOM 417 CB PHE A 89 10.600 34.667 25.069 1.00 24.95 C ATOM 418 CG PHE A 89 11.445 35.798 24.548 1.00 35.29 C ATOM 419 CD1 PHE A 89 10.856 36.922 23.979 1.00 30.45 C ATOM 420 CD2 PHE A 89 12.829 35.759 24.664 1.00 30.00 C ATOM 421 CE1 PHE A 89 11.635 37.972 23.514 1.00 34.44 C ATOM 422 CE2 PHE A 89 13.611 36.806 24.205 1.00 25.71 C ATOM 423 CZ PHE A 89 13.015 37.914 23.629 1.00 28.68 C ATOM 424 N GLY A 90 9.304 32.718 27.336 1.00 27.60 N ATOM 425 CA GLY A 90 8.275 31.839 27.861 1.00 28.50 C ATOM 426 C GLY A 90 7.575 32.405 29.088 1.00 39.02 C ATOM 427 O GLY A 90 6.375 32.197 29.275 1.00 32.04 O ATOM 428 N ALA A 91 8.334 33.115 29.923 1.00 38.17 N ATOM 429 CA ALA A 91 7.785 33.807 31.090 1.00 38.01 C ATOM 430 C ALA A 91 6.778 34.904 30.712 1.00 41.93 C ATOM 431 O ALA A 91 5.712 35.003 31.324 1.00 38.41 O ATOM 432 CB ALA A 91 8.897 34.385 31.945 1.00 23.78 C ATOM 433 N THR A 92 7.109 35.725 29.715 1.00 30.25 N ATOM 434 CA THR A 92 6.186 36.772 29.268 1.00 36.62 C ATOM 435 C THR A 92 4.868 36.163 28.810 1.00 39.14 C ATOM 436 O THR A 92 3.800 36.710 29.069 1.00 47.30 O ATOM 437 CB THR A 92 6.772 37.655 28.130 1.00 32.74 C ATOM 438 OG1 THR A 92 7.053 36.848 26.981 1.00 30.04 O ATOM 439 CG2 THR A 92 8.059 38.351 28.584 1.00 36.00 C ATOM 440 N LEU A 93 4.951 35.014 28.148 1.00 36.28 N ATOM 441 CA LEU A 93 3.772 34.333 27.632 1.00 39.12 C ATOM 442 C LEU A 93 2.872 33.778 28.751 1.00 44.75 C ATOM 443 O LEU A 93 1.691 34.115 28.847 1.00 41.41 O ATOM 444 CB LEU A 93 4.201 33.209 26.687 1.00 35.20 C ATOM 445 CG LEU A 93 3.092 32.349 26.076 1.00 35.90 C ATOM 446 CD1 LEU A 93 2.183 33.185 25.189 1.00 33.51 C ATOM 447 CD2 LEU A 93 3.696 31.221 25.285 1.00 30.48 C ATOM 448 N VAL A 94 3.431 32.920 29.594 1.00 42.39 N ATOM 449 CA VAL A 94 2.649 32.328 30.665 1.00 51.25 C ATOM 450 C VAL A 94 2.018 33.418 31.533 1.00 50.02 C ATOM 451 O VAL A 94 0.849 33.334 31.893 1.00 48.69 O ATOM 452 CB VAL A 94 3.493 31.362 31.527 1.00 48.13 C ATOM 453 CG1 VAL A 94 2.611 30.651 32.526 1.00 49.23 C ATOM 454 CG2 VAL A 94 4.189 30.340 30.646 1.00 46.44 C ATOM 455 N VAL A 95 2.791 34.447 31.858 1.00 47.59 N ATOM 456 CA VAL A 95 2.266 35.553 32.651 1.00 51.50 C ATOM 457 C VAL A 95 1.266 36.409 31.870 1.00 51.68 C ATOM 458 O VAL A 95 0.073 36.329 32.121 1.00 58.48 O ATOM 459 CB VAL A 95 3.388 36.435 33.250 1.00 56.92 C ATOM 460 CG1 VAL A 95 2.827 37.763 33.744 1.00 56.56 C ATOM 461 CG2 VAL A 95 4.095 35.701 34.387 1.00 51.83 C ATOM 462 N ARG A 96 1.728 37.224 30.925 1.00 47.61 N ATOM 463 CA ARG A 96 0.808 38.124 30.228 1.00 53.03 C ATOM 464 C ARG A 96 −0.325 37.375 29.491 1.00 55.31 C ATOM 465 O ARG A 96 −1.303 37.990 29.064 1.00 52.56 O ATOM 466 CB ARG A 96 1.555 39.099 29.299 1.00 52.24 C ATOM 467 CG ARG A 96 2.577 40.009 30.008 1.00 66.10 C ATOM 468 CD ARG A 96 2.120 41.476 30.244 1.00 77.39 C ATOM 469 NE ARG A 96 3.187 42.262 30.893 1.00 93.02 N ATOM 470 CZ ARG A 96 3.076 43.519 31.337 1.00 93.73 C ATOM 471 NH1 ARG A 96 1.928 44.174 31.210 1.00 91.80 N ATOM 472 NH2 ARG A 96 4.119 44.125 31.916 1.00 53.01 N ATOM 473 N GLY A 97 −0.197 36.054 29.354 1.00 47.46 N ATOM 474 CA GLY A 97 −1.247 35.245 28.760 1.00 35.30 C ATOM 475 C GLY A 97 −1.342 35.342 27.244 1.00 45.82 C ATOM 476 O GLY A 97 −2.318 34.899 26.644 1.00 44.15 O ATOM 477 N THR A 98 −0.323 35.910 26.613 1.00 49.47 N ATOM 478 CA THR A 98 −0.352 36.123 25.165 1.00 48.86 C ATOM 479 C THR A 98 1.056 36.232 24.593 1.00 44.15 C ATOM 480 O THR A 98 1.990 36.624 25.306 1.00 44.96 O ATOM 481 CB THR A 98 −1.163 37.382 24.812 1.00 42.13 C ATOM 482 OG1 THR A 98 −2.472 36.989 24.387 1.00 55.31 O ATOM 483 CG2 THR A 98 −0.495 38.163 23.696 1.00 45.21 C ATOM 484 N TRP A 99 1.215 35.863 23.321 1.00 32.98 N ATOM 485 CA TRP A 99 2.506 36.013 22.658 1.00 35.42 C ATOM 486 C TRP A 99 2.677 37.422 22.133 1.00 30.32 C ATOM 487 O TRP A 99 1.857 37.895 21.365 1.00 32.08 O ATOM 488 CB TRP A 99 2.706 35.019 21.525 1.00 29.63 C ATOM 489 CG TRP A 99 4.077 35.143 20.972 1.00 31.98 C ATOM 490 CD1 TRP A 99 4.446 35.779 19.825 1.00 31.71 C ATOM 491 CD2 TRP A 99 5.284 34.663 21.571 1.00 34.38 C ATOM 492 NE1 TRP A 99 5.803 35.705 19.656 1.00 27.86 N ATOM 493 CE2 TRP A 99 6.346 35.021 20.714 1.00 39.18 C ATOM 494 CE3 TRP A 99 5.571 33.956 22.743 1.00 29.09 C ATOM 495 CZ2 TRP A 99 7.678 34.699 20.993 1.00 30.71 C ATOM 496 CZ3 TRP A 99 6.892 33.626 23.015 1.00 29.99 C ATOM 497 CH2 TRP A 99 7.928 34.002 22.145 1.00 26.55 C ATOM 498 N LEU A 100 3.760 38.077 22.553 1.00 36.74 N ATOM 499 CA LEU A 100 3.926 39.520 22.367 1.00 33.47 C ATOM 500 C LEU A 100 4.969 39.874 21.324 1.00 32.65 C ATOM 501 O LEU A 100 5.250 41.050 21.089 1.00 37.27 O ATOM 502 CB LEU A 100 4.318 40.181 23.695 1.00 32.20 C ATOM 503 CG LEU A 100 3.287 40.176 24.819 1.00 46.27 C ATOM 504 CD1 LEU A 100 3.875 40.752 26.100 1.00 41.60 C ATOM 505 CD2 LEU A 100 2.047 40.949 24.394 1.00 30.59 C ATOM 506 N TRP A 101 5.557 38.869 20.695 1.00 29.12 N ATOM 507 CA TRP A 101 6.748 39.127 19.903 1.00 29.88 C ATOM 508 C TRP A 101 6.606 38.914 18.388 1.00 34.11 C ATOM 509 O TRP A 101 7.568 39.096 17.647 1.00 39.62 O ATOM 510 CB TRP A 101 7.920 38.333 20.484 1.00 31.13 C ATOM 511 CG TRP A 101 8.061 38.565 21.956 1.00 27.78 C ATOM 512 CD1 TRP A 101 7.501 37.829 22.964 1.00 31.52 C ATOM 513 CD2 TRP A 101 8.788 39.616 22.590 1.00 29.18 C ATOM 514 NE1 TRP A 101 7.837 38.357 24.181 1.00 27.82 N ATOM 515 CE2 TRP A 101 8.627 39.454 23.983 1.00 25.81 C ATOM 516 CE3 TRP A 101 9.571 40.668 22.116 1.00 27.74 C ATOM 517 CZ2 TRP A 101 9.214 40.303 24.901 1.00 25.77 C ATOM 518 CZ3 TRP A 101 10.154 41.514 23.032 1.00 33.88 C ATOM 519 CH2 TRP A 101 9.972 41.329 24.411 1.00 38.30 C ATOM 520 N GLY A 102 5.417 38.549 17.921 1.00 39.83 N ATOM 521 CA GLY A 102 5.217 38.324 16.499 1.00 41.12 C ATOM 522 C GLY A 102 5.430 36.870 16.133 1.00 41.74 C ATOM 523 O GLY A 102 6.134 36.147 16.834 1.00 41.56 O ATOM 524 N SER A 103 4.834 36.440 15.025 1.00 52.63 N ATOM 525 CA SER A 103 4.799 35.014 14.687 1.00 52.56 C ATOM 526 C SER A 103 6.164 34.397 14.345 1.00 41.54 C ATOM 527 O SER A 103 6.422 33.241 14.685 1.00 44.48 O ATOM 528 CB SER A 103 3.772 34.731 13.589 1.00 35.57 C ATOM 529 OG SER A 103 3.929 35.636 12.518 1.00 50.88 O ATOM 530 N PHE A 104 7.040 35.155 13.694 1.00 33.70 N ATOM 531 CA PHE A 104 8.385 34.646 13.422 1.00 38.78 C ATOM 532 C PHE A 104 9.219 34.343 14.677 1.00 39.60 C ATOM 533 O PHE A 104 9.855 33.282 14.781 1.00 26.66 O ATOM 534 CB PHE A 104 9.182 35.604 12.552 1.00 35.33 C ATOM 535 CG PHE A 104 10.600 35.188 12.388 1.00 32.63 C ATOM 536 CD1 PHE A 104 10.943 34.227 11.450 1.00 32.98 C ATOM 537 CD2 PHE A 104 11.589 35.714 13.205 1.00 38.27 C ATOM 538 CE1 PHE A 104 12.259 33.814 11.308 1.00 42.26 C ATOM 539 CE2 PHE A 104 12.910 35.315 13.068 1.00 38.99 C ATOM 540 CZ PHE A 104 13.245 34.360 12.120 1.00 36.71 C ATOM 541 N LEU A 105 9.248 35.291 15.609 1.00 32.02 N ATOM 542 CA LEU A 105 9.966 35.076 16.854 1.00 32.42 C ATOM 543 C LEU A 105 9.352 33.914 17.634 1.00 31.91 C ATOM 544 O LEU A 105 10.056 33.184 18.333 1.00 21.66 O ATOM 545 CB LEU A 105 10.017 36.356 17.681 1.00 32.02 C ATOM 546 CG LEU A 105 11.105 37.322 17.208 1.00 32.23 C ATOM 547 CD1 LEU A 105 11.122 38.608 18.042 1.00 27.17 C ATOM 548 CD2 LEU A 105 12.455 36.630 17.228 1.00 25.20 C ATOM 549 N CYS A 106 8.043 33.731 17.489 1.00 28.81 N ATOM 550 CA CYS A 106 7.383 32.573 18.069 1.00 24.29 C ATOM 551 C CYS A 106 7.949 31.277 17.484 1.00 28.87 C ATOM 552 O CYS A 106 8.253 30.329 18.211 1.00 23.80 O ATOM 553 CB CYS A 106 5.874 32.642 17.851 1.00 29.79 C ATOM 554 SG CYS A 106 5.004 31.087 18.158 1.00 29.48 S ATOM 555 N GLU A 107 8.113 31.235 16.168 1.00 29.13 N ATOM 556 CA GLU A 107 8.623 30.024 15.535 1.00 25.62 C ATOM 557 C GLU A 107 10.128 29.835 15.734 1.00 25.27 C ATOM 558 O GLU A 107 10.605 28.706 15.860 1.00 20.16 O ATOM 559 CB GLU A 107 8.231 29.975 14.064 1.00 27.94 C ATOM 560 CG GLU A 107 6.746 29.796 13.873 1.00 26.15 C ATOM 561 CD GLU A 107 6.289 30.081 12.462 1.00 37.99 C ATOM 562 OE1 GLU A 107 7.015 29.720 11.518 1.00 49.31 O ATOM 563 OE2 GLU A 107 5.192 30.660 12.292 1.00 52.40 O ATOM 564 N LEU A 108 10.872 30.937 15.790 1.00 21.61 N ATOM 565 CA LEU A 108 12.284 30.857 16.160 1.00 27.69 C ATOM 566 C LEU A 108 12.479 30.375 17.613 1.00 31.99 C ATOM 567 O LEU A 108 13.351 29.542 17.897 1.00 25.09 O ATOM 568 CB LEU A 108 12.975 32.200 15.940 1.00 25.86 C ATOM 569 CG LEU A 108 14.450 32.182 16.347 1.00 25.53 C ATOM 570 CD1 LEU A 108 15.156 30.996 15.695 1.00 22.16 C ATOM 571 CD2 LEU A 108 15.140 33.512 16.017 1.00 18.26 C ATOM 572 N TRP A 109 11.649 30.913 18.510 1.00 26.41 N ATOM 573 CA TRP A 109 11.617 30.561 19.930 1.00 23.93 C ATOM 574 C TRP A 109 11.379 29.072 20.166 1.00 32.19 C ATOM 575 O TRP A 109 12.103 28.426 20.932 1.00 29.43 O ATOM 576 CB TRP A 109 10.504 31.349 20.621 1.00 21.63 C ATOM 577 CG TRP A 109 10.321 31.016 22.063 1.00 25.45 C ATOM 578 CD1 TRP A 109 11.231 31.196 23.065 1.00 22.97 C ATOM 579 CD2 TRP A 109 9.146 30.470 22.682 1.00 32.06 C ATOM 580 NE1 TRP A 109 10.707 30.777 24.263 1.00 25.31 N ATOM 581 CE2 TRP A 109 9.429 30.328 24.062 1.00 27.98 C ATOM 582 CE3 TRP A 109 7.885 30.077 22.205 1.00 26.29 C ATOM 583 CZ2 TRP A 109 8.499 29.811 24.972 1.00 27.53 C ATOM 584 CZ3 TRP A 109 6.961 29.561 23.114 1.00 31.36 C ATOM 585 CH2 TRP A 109 7.274 29.439 24.483 1.00 27.80 C ATOM 586 N THR A 110 10.340 28.551 19.518 1.00 23.31 N ATOM 587 CA THR A 110 9.979 27.150 19.608 1.00 23.07 C ATOM 588 C THR A 110 11.140 26.285 19.146 1.00 30.79 C ATOM 589 O THR A 110 11.398 25.196 19.686 1.00 18.74 O ATOM 590 CB THR A 110 8.766 26.864 18.708 1.00 27.49 C ATOM 591 OG1 THR A 110 7.652 27.626 19.174 1.00 27.85 O ATOM 592 CG2 THR A 110 8.396 25.372 18.705 1.00 16.96 C ATOM 593 N SER A 111 11.827 26.787 18.125 1.00 30.93 N ATOM 594 CA SER A 111 13.000 26.134 17.564 1.00 29.34 C ATOM 595 C SER A 111 14.124 25.964 18.584 1.00 32.82 C ATOM 596 O SER A 111 14.658 24.864 18.745 1.00 29.79 O ATOM 597 CB SER A 111 13.527 26.950 16.387 1.00 30.22 C ATOM 598 OG SER A 111 12.801 26.664 15.207 1.00 49.18 O ATOM 599 N LEU A 112 14.488 27.061 19.250 1.00 25.83 N ATOM 600 CA LEU A 112 15.567 27.046 20.227 1.00 22.76 C ATOM 601 C LEU A 112 15.179 26.150 21.395 1.00 24.47 C ATOM 602 O LEU A 112 15.998 25.405 21.939 1.00 20.91 O ATOM 603 CB LEU A 112 15.880 28.470 20.692 1.00 17.00 C ATOM 604 CG LEU A 112 16.298 29.405 19.552 1.00 25.17 C ATOM 605 CD1 LEU A 112 16.361 30.866 19.971 1.00 18.57 C ATOM 606 CD2 LEU A 112 17.628 28.963 18.962 1.00 18.70 C ATOM 607 N ASP A 113 13.909 26.205 21.762 1.00 17.82 N ATOM 608 CA ASP A 113 13.410 25.374 22.837 1.00 20.69 C ATOM 609 C ASP A 113 13.584 23.889 22.484 1.00 25.82 C ATOM 610 O ASP A 113 14.059 23.104 23.302 1.00 27.43 O ATOM 611 CB ASP A 113 11.951 25.724 23.101 1.00 20.34 C ATOM 612 CG ASP A 113 11.414 25.091 24.344 1.00 20.22 C ATOM 613 OD1 ASP A 113 11.950 24.070 24.800 1.00 25.57 O ATOM 614 OD2 ASP A 113 10.435 25.621 24.874 1.00 28.51 O ATOM 615 N VAL A 114 13.226 23.521 21.256 1.00 22.54 N ATOM 616 CA VAL A 114 13.399 22.151 20.771 1.00 23.64 C ATOM 617 C VAL A 114 14.872 21.729 20.637 1.00 25.12 C ATOM 618 O VAL A 114 15.255 20.621 21.044 1.00 24.22 O ATOM 619 CB VAL A 114 12.679 21.952 19.425 1.00 21.36 C ATOM 620 CG1 VAL A 114 12.823 20.526 18.949 1.00 21.22 C ATOM 621 CG2 VAL A 114 11.223 22.292 19.577 1.00 25.23 C ATOM 622 N LEU A 115 15.684 22.616 20.068 1.00 18.85 N ATOM 623 CA LEU A 115 17.131 22.430 19.966 1.00 17.94 C ATOM 624 C LEU A 115 17.785 22.008 21.272 1.00 30.95 C ATOM 625 O LEU A 115 18.519 21.007 21.323 1.00 23.36 O ATOM 626 CB LEU A 115 17.780 23.735 19.515 1.00 17.88 C ATOM 627 CG LEU A 115 19.278 23.694 19.229 1.00 28.01 C ATOM 628 CD1 LEU A 115 19.590 22.744 18.083 1.00 20.89 C ATOM 629 CD2 LEU A 115 19.779 25.092 18.928 1.00 23.88 C ATOM 630 N CYS A 116 17.512 22.784 22.325 1.00 32.44 N ATOM 631 CA CYS A 116 18.230 22.675 23.586 1.00 20.80 C ATOM 632 C CYS A 116 17.958 21.361 24.305 1.00 23.94 C ATOM 633 O CYS A 116 18.884 20.718 24.797 1.00 26.96 O ATOM 634 CB CYS A 116 17.916 23.872 24.475 1.00 25.38 C ATOM 635 SG CYS A 116 18.713 25.395 23.919 1.00 33.66 S ATOM 636 N VAL A 117 16.698 20.948 24.355 1.00 17.87 N ATOM 637 CA VAL A 117 16.364 19.634 24.900 1.00 18.68 C ATOM 638 C VAL A 117 17.058 18.527 24.103 1.00 21.45 C ATOM 639 O VAL A 117 17.612 17.592 24.669 1.00 16.69 O ATOM 640 CB VAL A 117 14.838 19.376 24.867 1.00 19.25 C ATOM 641 CG1 VAL A 117 14.498 18.031 25.492 1.00 15.98 C ATOM 642 CG2 VAL A 117 14.108 20.484 25.560 1.00 21.84 C ATOM 643 N THR A 118 17.021 18.641 22.778 1.00 24.64 N ATOM 644 CA THR A 118 17.640 17.655 21.907 1.00 23.06 C ATOM 645 C THR A 118 19.159 17.585 22.086 1.00 22.58 C ATOM 646 O THR A 118 19.723 16.500 22.249 1.00 19.86 O ATOM 647 CB THR A 118 17.290 17.943 20.446 1.00 25.18 C ATOM 648 OG1 THR A 118 15.862 17.976 20.316 1.00 31.14 O ATOM 649 CG2 THR A 118 17.865 16.872 19.531 1.00 21.94 C ATOM 650 N ALA A 119 19.818 18.738 22.074 1.00 13.86 N ATOM 651 CA ALA A 119 21.259 18.755 22.259 1.00 16.35 C ATOM 652 C ALA A 119 21.682 18.219 23.644 1.00 25.85 C ATOM 653 O ALA A 119 22.705 17.546 23.765 1.00 23.32 O ATOM 654 CB ALA A 119 21.805 20.155 22.031 1.00 17.40 C ATOM 655 N SER A 120 20.906 18.527 24.685 1.00 19.69 N ATOM 656 CA SER A 120 21.248 18.111 26.039 1.00 17.57 C ATOM 657 C SER A 120 21.300 16.601 26.146 1.00 22.49 C ATOM 658 O SER A 120 22.303 16.030 26.580 1.00 22.20 O ATOM 659 CB SER A 120 20.245 18.651 27.051 1.00 17.38 C ATOM 660 OG SER A 120 20.324 20.062 27.147 1.00 26.82 O ATOM 661 N ILE A 121 20.210 15.960 25.735 1.00 23.45 N ATOM 662 CA ILE A 121 20.060 14.523 25.876 1.00 21.41 C ATOM 663 C ILE A 121 21.031 13.795 24.948 1.00 21.50 C ATOM 664 O ILE A 121 21.508 12.709 25.260 1.00 29.42 O ATOM 665 CB ILE A 121 18.611 14.095 25.624 1.00 20.38 C ATOM 666 CG1 ILE A 121 18.468 12.579 25.712 1.00 23.98 C ATOM 667 CG2 ILE A 121 18.152 14.596 24.270 1.00 25.87 C ATOM 668 CD1 ILE A 121 19.035 11.994 26.963 1.00 19.99 C ATOM 669 N GLU A 122 21.352 14.391 23.813 1.00 19.49 N ATOM 670 CA GLU A 122 22.384 13.796 22.977 1.00 25.68 C ATOM 671 C GLU A 122 23.759 13.899 23.666 1.00 26.31 C ATOM 672 O GLU A 122 24.495 12.916 23.768 1.00 23.49 O ATOM 673 CB GLU A 122 22.380 14.414 21.573 1.00 24.16 C ATOM 674 CG GLU A 122 21.217 13.928 20.708 1.00 36.65 C ATOM 675 CD GLU A 122 21.259 14.435 19.266 1.00 51.16 C ATOM 676 OE1 GLU A 122 22.372 14.562 18.699 1.00 53.58 O ATOM 677 OE2 GLU A 122 20.169 14.684 18.693 1.00 43.13 O ATOM 678 N THR A 123 24.082 15.085 24.167 1.00 20.57 N ATOM 679 CA THR A 123 25.325 15.289 24.890 1.00 20.18 C ATOM 680 C THR A 123 25.466 14.333 26.084 1.00 26.78 C ATOM 681 O THR A 123 26.564 13.863 26.389 1.00 24.79 O ATOM 682 CB THR A 123 25.486 16.753 25.346 1.00 24.64 C ATOM 683 OG1 THR A 123 25.525 17.621 24.202 1.00 26.06 O ATOM 684 CG2 THR A 123 26.769 16.930 26.136 1.00 26.04 C ATOM 685 N LEU A 124 24.356 14.034 26.753 1.00 24.32 N ATOM 686 CA LEU A 124 24.380 13.087 27.865 1.00 19.80 C ATOM 687 C LEU A 124 24.688 11.676 27.383 1.00 28.83 C ATOM 688 O LEU A 124 25.385 10.930 28.066 1.00 27.68 O ATOM 689 CB LEU A 124 23.056 13.092 28.633 1.00 22.50 C ATOM 690 CG LEU A 124 22.785 14.283 29.554 1.00 25.11 C ATOM 691 CD1 LEU A 124 21.442 14.145 30.238 1.00 24.23 C ATOM 692 CD2 LEU A 124 23.878 14.441 30.574 1.00 18.69 C ATOM 693 N CYS A 125 24.158 11.305 26.220 1.00 26.56 N ATOM 694 CA CYS A 125 24.519 10.046 25.580 1.00 30.82 C ATOM 695 C CYS A 125 26.018 9.922 25.363 1.00 31.05 C ATOM 696 O CYS A 125 26.629 8.917 25.731 1.00 28.69 O ATOM 697 CB CYS A 125 23.847 9.935 24.221 1.00 31.32 C ATOM 698 SG CYS A 125 22.263 9.213 24.305 1.00 49.40 S ATOM 699 N VAL A 126 26.593 10.944 24.734 1.00 25.97 N ATOM 700 CA VAL A 126 28.018 10.962 24.434 1.00 30.63 C ATOM 701 C VAL A 126 28.825 10.813 25.719 1.00 32.81 C ATOM 702 O VAL A 126 29.790 10.058 25.762 1.00 35.10 O ATOM 703 CB VAL A 126 28.428 12.267 23.720 1.00 34.42 C ATOM 704 CG1 VAL A 126 29.943 12.426 23.715 1.00 26.18 C ATOM 705 CG2 VAL A 126 27.851 12.316 22.303 1.00 22.68 C ATOM 706 N ILE A 127 28.419 11.529 26.765 1.00 27.77 N ATOM 707 CA ILE A 127 29.070 11.407 28.061 1.00 29.29 C ATOM 708 C ILE A 127 29.058 9.966 28.612 1.00 31.65 C ATOM 709 O ILE A 127 30.076 9.478 29.093 1.00 35.89 O ATOM 710 CB ILE A 127 28.484 12.399 29.081 1.00 29.77 C ATOM 711 CG1 ILE A 127 28.858 13.832 28.695 1.00 21.67 C ATOM 712 CG2 ILE A 127 28.990 12.087 30.474 1.00 23.05 C ATOM 713 CD1 ILE A 127 28.046 14.880 29.383 1.00 19.91 C ATOM 714 N ALA A 128 27.922 9.282 28.525 1.00 27.16 N ATOM 715 CA ALA A 128 27.853 7.877 28.927 1.00 31.35 C ATOM 716 C ALA A 128 28.800 6.995 28.109 1.00 34.42 C ATOM 717 O ALA A 128 29.569 6.218 28.661 1.00 42.98 O ATOM 718 CB ALA A 128 26.424 7.354 28.821 1.00 32.42 C ATOM 719 N ILE A 129 28.724 7.110 26.794 1.00 25.63 N ATOM 720 CA ILE A 129 29.538 6.302 25.893 1.00 32.80 C ATOM 721 C ILE A 129 31.041 6.551 26.100 1.00 39.23 C ATOM 722 O ILE A 129 31.850 5.622 26.050 1.00 35.36 O ATOM 723 CB ILE A 129 29.122 6.552 24.408 1.00 31.99 C ATOM 724 CG1 ILE A 129 27.817 5.821 24.100 1.00 25.34 C ATOM 725 CG2 ILE A 129 30.215 6.134 23.431 1.00 18.91 C ATOM 726 CD1 ILE A 129 27.126 6.327 22.883 1.00 16.13 C ATOM 727 N ASP A 130 31.395 7.810 26.343 1.00 36.21 N ATOM 728 CA ASP A 130 32.777 8.232 26.540 1.00 32.64 C ATOM 729 C ASP A 130 33.348 7.576 27.792 1.00 39.60 C ATOM 730 O ASP A 130 34.435 6.995 27.757 1.00 39.45 O ATOM 731 CB ASP A 130 32.822 9.770 26.638 1.00 44.57 C ATOM 732 CG ASP A 130 34.147 10.311 27.188 1.00 57.37 C ATOM 733 OD1 ASP A 130 35.171 10.292 26.462 1.00 55.76 O ATOM 734 OD2 ASP A 130 34.149 10.804 28.342 1.00 45.48 O ATOM 735 N ARG A 131 32.598 7.660 28.891 1.00 40.43 N ATOM 736 CA ARG A 131 32.989 7.030 30.152 1.00 40.13 C ATOM 737 C ARG A 131 33.063 5.504 30.036 1.00 34.50 C ATOM 738 O ARG A 131 34.053 4.896 30.425 1.00 44.83 O ATOM 739 CB ARG A 131 32.048 7.450 31.289 1.00 29.24 C ATOM 740 CG ARG A 131 32.278 8.875 31.807 1.00 34.21 C ATOM 741 CD ARG A 131 33.714 9.113 32.252 1.00 37.61 C ATOM 742 NE ARG A 131 34.599 9.430 31.137 1.00 43.94 N ATOM 743 CZ ARG A 131 35.926 9.381 31.194 1.00 48.00 C ATOM 744 NH1 ARG A 131 36.532 9.017 32.314 1.00 59.85 N ATOM 745 NH2 ARG A 131 36.650 9.691 30.129 1.00 49.97 N ATOM 746 N TYR A 132 32.018 4.887 29.504 1.00 28.51 N ATOM 747 CA TYR A 132 32.041 3.454 29.255 1.00 41.61 C ATOM 748 C TYR A 132 33.282 2.996 28.485 1.00 45.44 C ATOM 749 O TYR A 132 33.866 1.958 28.792 1.00 43.33 O ATOM 750 CB TYR A 132 30.790 3.021 28.494 1.00 40.24 C ATOM 751 CG TYR A 132 30.865 1.588 28.040 1.00 50.36 C ATOM 752 CD1 TYR A 132 30.509 0.552 28.894 1.00 50.22 C ATOM 753 CD2 TYR A 132 31.318 1.267 26.765 1.00 50.69 C ATOM 754 CE1 TYR A 132 30.584 −0.761 28.490 1.00 48.44 C ATOM 755 CE2 TYR A 132 31.394 −0.047 26.349 1.00 49.88 C ATOM 756 CZ TYR A 132 31.025 −1.054 27.216 1.00 55.07 C ATOM 757 OH TYR A 132 31.104 −2.363 26.815 1.00 71.99 O ATOM 758 N LEU A 133 33.673 3.763 27.474 1.00 40.17 N ATOM 759 CA LEU A 133 34.835 3.408 26.663 1.00 43.76 C ATOM 760 C LEU A 133 36.148 3.710 27.372 1.00 52.16 C ATOM 761 O LEU A 133 37.132 3.002 27.181 1.00 57.70 O ATOM 762 CB LEU A 133 34.799 4.096 25.295 1.00 42.37 C ATOM 763 CG LEU A 133 33.717 3.594 24.329 1.00 49.80 C ATOM 764 CD1 LEU A 133 33.781 4.345 23.016 1.00 24.35 C ATOM 765 CD2 LEU A 133 33.801 2.086 24.088 1.00 43.34 C ATOM 766 N ALA A 134 36.164 4.753 28.193 1.00 44.11 N ATOM 767 CA ALA A 134 37.358 5.071 28.958 1.00 41.10 C ATOM 768 C ALA A 134 37.628 4.007 30.021 1.00 52.54 C ATOM 769 O ALA A 134 38.697 3.985 30.635 1.00 60.51 O ATOM 770 CB ALA A 134 37.236 6.439 29.595 1.00 32.00 C ATOM 771 N ILE A 135 36.667 3.108 30.218 1.00 50.87 N ATOM 772 CA ILE A 135 36.682 2.230 31.384 1.00 57.17 C ATOM 773 C ILE A 135 36.814 0.749 31.050 1.00 50.48 C ATOM 774 O ILE A 135 36.780 −0.092 31.937 1.00 64.50 O ATOM 775 CB ILE A 135 35.408 2.425 32.229 1.00 49.89 C ATOM 776 CG1 ILE A 135 35.746 2.550 33.710 1.00 53.84 C ATOM 777 CG2 ILE A 135 34.430 1.291 32.013 1.00 51.13 C ATOM 778 CD1 ILE A 135 34.508 2.637 34.585 1.00 61.01 C ATOM 779 N THR A 136 36.961 0.429 29.775 1.00 56.71 N ATOM 780 CA THR A 136 37.014 −0.965 29.349 1.00 61.77 C ATOM 781 C THR A 136 38.064 −1.155 28.257 1.00 68.81 C ATOM 782 O THR A 136 38.435 −2.278 27.911 1.00 68.01 O ATOM 783 CB THR A 136 35.634 −1.452 28.828 1.00 62.73 C ATOM 784 OG1 THR A 136 35.207 −0.633 27.735 1.00 53.79 O ATOM 785 CG2 THR A 136 34.587 −1.389 29.926 1.00 57.04 C ATOM 786 N SER A 137 38.542 −0.037 27.724 1.00 59.43 N ATOM 787 CA SER A 137 39.503 −0.042 26.639 1.00 61.67 C ATOM 788 C SER A 137 40.381 1.188 26.793 1.00 54.76 C ATOM 789 O SER A 137 40.530 1.965 25.849 1.00 51.16 O ATOM 790 CB SER A 137 38.763 0.009 25.299 1.00 57.88 C ATOM 791 OG SER A 137 37.514 −0.661 25.392 1.00 52.55 O ATOM 792 N PRO A 138 40.971 1.362 27.989 1.00 50.19 N ATOM 793 CA PRO A 138 41.644 2.604 28.394 1.00 51.45 C ATOM 794 C PRO A 138 42.815 2.962 27.493 1.00 55.73 C ATOM 795 O PRO A 138 43.122 4.145 27.331 1.00 53.65 O ATOM 796 CB PRO A 138 42.152 2.294 29.809 1.00 45.34 C ATOM 797 CG PRO A 138 41.438 1.061 30.236 1.00 47.72 C ATOM 798 CD PRO A 138 41.147 0.295 28.984 1.00 50.12 C ATOM 799 N PHE A 139 43.472 1.959 26.919 1.00 58.57 N ATOM 800 CA PHE A 139 44.595 2.247 26.041 1.00 58.56 C ATOM 801 C PHE A 139 44.075 2.902 24.790 1.00 55.67 C ATOM 802 O PHE A 139 44.411 4.048 24.486 1.00 52.96 O ATOM 803 CB PHE A 139 45.364 0.990 25.660 1.00 59.59 C ATOM 804 CG PHE A 139 46.527 1.262 24.754 1.00 60.38 C ATOM 805 CD1 PHE A 139 47.688 1.832 25.251 1.00 59.05 C ATOM 806 CD2 PHE A 139 46.454 0.969 23.401 1.00 64.77 C ATOM 807 CE1 PHE A 139 48.759 2.091 24.420 1.00 63.99 C ATOM 808 CE2 PHE A 139 47.520 1.225 22.563 1.00 62.51 C ATOM 809 CZ PHE A 139 48.675 1.787 23.072 1.00 67.11 C ATOM 810 N ARG A 140 43.250 2.153 24.067 1.00 62.52 N ATOM 811 CA ARG A 140 42.610 2.657 22.859 1.00 65.01 C ATOM 812 C ARG A 140 41.910 3.981 23.147 1.00 54.59 C ATOM 813 O ARG A 140 41.828 4.848 22.283 1.00 50.00 O ATOM 814 CB ARG A 140 41.627 1.626 22.292 1.00 64.66 C ATOM 815 CG ARG A 140 42.298 0.427 21.627 1.00 72.71 C ATOM 816 CD ARG A 140 41.275 −0.501 20.988 1.00 92.46 C ATOM 817 NE ARG A 140 41.848 −1.265 19.883 1.00 114.69 N ATOM 818 CZ ARG A 140 41.138 −2.003 19.034 1.00 128.89 C ATOM 819 NH1 ARG A 140 39.820 −2.082 19.164 1.00 121.02 N ATOM 820 NH2 ARG A 140 41.746 −2.662 18.052 1.00 132.20 N ATOM 821 N TYR A 141 41.426 4.143 24.373 1.00 44.20 N ATOM 822 CA TYR A 141 40.816 5.399 24.752 1.00 40.46 C ATOM 823 C TYR A 141 41.834 6.528 24.845 1.00 47.63 C ATOM 824 O TYR A 141 41.626 7.586 24.267 1.00 52.61 O ATOM 825 CB TYR A 141 40.042 5.277 26.058 1.00 45.22 C ATOM 826 CG TYR A 141 39.399 6.576 26.438 1.00 46.78 C ATOM 827 CD1 TYR A 141 38.080 6.836 26.116 1.00 50.94 C ATOM 828 CD2 TYR A 141 40.125 7.561 27.082 1.00 50.04 C ATOM 829 CE1 TYR A 141 37.494 8.039 26.451 1.00 58.26 C ATOM 830 CE2 TYR A 141 39.553 8.761 27.419 1.00 56.11 C ATOM 831 CZ TYR A 141 38.239 8.999 27.104 1.00 58.99 C ATOM 832 OH TYR A 141 37.674 10.207 27.445 1.00 67.52 O ATOM 833 N GLN A 142 42.927 6.313 25.573 1.00 60.74 N ATOM 834 CA GLN A 142 43.962 7.346 25.709 1.00 61.14 C ATOM 835 C GLN A 142 44.581 7.704 24.359 1.00 50.67 C ATOM 836 O GLN A 142 45.029 8.831 24.150 1.00 48.73 O ATOM 837 CB GLN A 142 45.070 6.928 26.688 1.00 43.75 C ATOM 838 CG GLN A 142 44.635 6.778 28.135 1.00 66.68 C ATOM 839 CD GLN A 142 44.155 8.087 28.750 1.00 85.90 C ATOM 840 OE1 GLN A 142 44.232 9.144 28.121 1.00 83.34 O ATOM 841 NE2 GLN A 142 43.653 8.020 29.987 1.00 78.62 N ATOM 842 N SER A 143 44.603 6.747 23.441 1.00 39.96 N ATOM 843 CA SER A 143 45.270 6.974 22.164 1.00 59.02 C ATOM 844 C SER A 143 44.382 7.607 21.077 1.00 57.13 C ATOM 845 O SER A 143 44.893 8.197 20.128 1.00 52.88 O ATOM 846 CB SER A 143 45.942 5.692 21.658 1.00 58.12 C ATOM 847 OG SER A 143 45.057 4.588 21.683 1.00 66.04 O ATOM 848 N LEU A 144 43.065 7.503 21.219 1.00 54.42 N ATOM 849 CA LEU A 144 42.153 8.080 20.228 1.00 49.61 C ATOM 850 C LEU A 144 41.529 9.399 20.665 1.00 52.78 C ATOM 851 O LEU A 144 41.476 10.346 19.887 1.00 43.31 O ATOM 852 CB LEU A 144 41.043 7.097 19.867 1.00 44.97 C ATOM 853 CG LEU A 144 41.571 5.805 19.263 1.00 58.94 C ATOM 854 CD1 LEU A 144 40.456 4.771 19.163 1.00 39.40 C ATOM 855 CD2 LEU A 144 42.216 6.096 17.913 1.00 44.96 C ATOM 856 N MET A 145 41.042 9.462 21.901 1.00 54.67 N ATOM 857 CA MET A 145 40.340 10.659 22.359 1.00 51.28 C ATOM 858 C MET A 145 41.272 11.802 22.735 1.00 43.78 C ATOM 859 O MET A 145 42.127 11.676 23.607 1.00 53.96 O ATOM 860 CB MET A 145 39.349 10.339 23.486 1.00 56.60 C ATOM 861 CG MET A 145 38.009 9.785 22.967 1.00 73.46 C ATOM 862 SD MET A 145 36.685 10.998 22.701 1.00 67.92 S ATOM 863 CE MET A 145 37.590 12.542 22.747 1.00 40.65 C ATOM 864 N THR A 146 41.091 12.919 22.047 1.00 38.95 N ATOM 865 CA THR A 146 41.873 14.117 22.283 1.00 39.32 C ATOM 866 C THR A 146 40.912 15.282 22.381 1.00 33.90 C ATOM 867 O THR A 146 39.720 15.119 22.148 1.00 48.32 O ATOM 868 CB THR A 146 42.864 14.377 21.120 1.00 47.11 C ATOM 869 OG1 THR A 146 42.145 14.666 19.910 1.00 36.97 O ATOM 870 CG2 THR A 146 43.727 13.159 20.893 1.00 40.04 C ATOM 871 N ARG A 147 41.435 16.464 22.687 1.00 38.18 N ATOM 872 CA ARG A 147 40.603 17.654 22.847 1.00 43.44 C ATOM 873 C ARG A 147 40.028 18.125 21.518 1.00 34.57 C ATOM 874 O ARG A 147 38.885 18.562 21.437 1.00 39.09 O ATOM 875 CB ARG A 147 41.401 18.789 23.493 1.00 42.59 C ATOM 876 CG ARG A 147 41.543 18.683 24.999 1.00 42.52 C ATOM 877 CD ARG A 147 42.184 19.938 25.549 1.00 53.25 C ATOM 878 NE ARG A 147 41.647 21.124 24.886 1.00 72.74 N ATOM 879 CZ ARG A 147 40.785 21.972 25.444 1.00 87.64 C ATOM 880 NH1 ARG A 147 40.368 21.772 26.691 1.00 62.96 N ATOM 881 NH2 ARG A 147 40.346 23.027 24.760 1.00 81.57 N ATOM 882 N ALA A 148 40.832 18.043 20.473 1.00 40.70 N ATOM 883 CA ALA A 148 40.380 18.440 19.147 1.00 40.53 C ATOM 884 C ALA A 148 39.252 17.527 18.702 1.00 40.03 C ATOM 885 O ALA A 148 38.280 17.974 18.088 1.00 33.02 O ATOM 886 CB ALA A 148 41.527 18.376 18.161 1.00 27.09 C ATOM 887 N ARG A 149 39.398 16.244 19.023 1.00 33.11 N ATOM 888 CA ARG A 149 38.413 15.251 18.654 1.00 28.79 C ATOM 889 C ARG A 149 37.094 15.460 19.375 1.00 34.20 C ATOM 890 O ARG A 149 36.022 15.474 18.754 1.00 30.21 O ATOM 891 CB ARG A 149 38.952 13.844 18.901 1.00 34.28 C ATOM 892 CG ARG A 149 39.189 13.106 17.606 1.00 27.64 C ATOM 893 CD ARG A 149 40.069 11.892 17.735 1.00 36.04 C ATOM 894 NE ARG A 149 41.030 11.886 16.635 1.00 45.94 N ATOM 895 CZ ARG A 149 42.053 11.050 16.526 1.00 47.53 C ATOM 896 NH1 ARG A 149 42.259 10.116 17.443 1.00 54.10 N ATOM 897 NH2 ARG A 149 42.868 11.148 15.491 1.00 50.77 N ATOM 898 N ALA A 150 37.180 15.622 20.687 1.00 33.01 N ATOM 899 CA ALA A 150 35.999 15.881 21.500 1.00 31.61 C ATOM 900 C ALA A 150 35.179 17.063 20.963 1.00 32.79 C ATOM 901 O ALA A 150 33.948 16.996 20.925 1.00 29.03 O ATOM 902 CB ALA A 150 36.402 16.112 22.934 1.00 27.20 C ATOM 903 N LYS A 151 35.864 18.131 20.544 1.00 26.42 N ATOM 904 CA LYS A 151 35.206 19.309 19.976 1.00 30.25 C ATOM 905 C LYS A 151 34.480 18.980 18.676 1.00 36.13 C ATOM 906 O LYS A 151 33.372 19.474 18.422 1.00 29.92 O ATOM 907 CB LYS A 151 36.203 20.450 19.763 1.00 25.66 C ATOM 908 CG LYS A 151 36.644 21.080 21.070 1.00 49.85 C ATOM 909 CD LYS A 151 37.619 22.227 20.865 1.00 62.10 C ATOM 910 CE LYS A 151 38.486 22.431 22.113 1.00 54.49 C ATOM 911 NZ LYS A 151 39.246 23.717 22.076 1.00 67.73 N ATOM 912 N VAL A 152 35.104 18.140 17.857 1.00 25.42 N ATOM 913 CA VAL A 152 34.441 17.653 16.663 1.00 28.28 C ATOM 914 C VAL A 152 33.142 16.954 17.067 1.00 25.71 C ATOM 915 O VAL A 152 32.084 17.245 16.519 1.00 31.29 O ATOM 916 CB VAL A 152 35.374 16.747 15.807 1.00 25.73 C ATOM 917 CG1 VAL A 152 34.596 15.941 14.780 1.00 16.62 C ATOM 918 CG2 VAL A 152 36.390 17.602 15.106 1.00 26.38 C ATOM 919 N ILE A 153 33.217 16.060 18.045 1.00 24.25 N ATOM 920 CA ILE A 153 32.032 15.356 18.531 1.00 25.84 C ATOM 921 C ILE A 153 30.935 16.295 19.059 1.00 25.44 C ATOM 922 O ILE A 153 29.753 16.092 18.786 1.00 28.98 O ATOM 923 CB ILE A 153 32.394 14.336 19.627 1.00 26.23 C ATOM 924 CG1 ILE A 153 33.361 13.291 19.079 1.00 20.10 C ATOM 925 CG2 ILE A 153 31.124 13.675 20.174 1.00 21.37 C ATOM 926 CD1 ILE A 153 34.241 12.652 20.136 1.00 16.51 C ATOM 927 N ILE A 154 31.325 17.313 19.814 1.00 19.46 N ATOM 928 CA ILE A 154 30.377 18.304 20.302 1.00 25.47 C ATOM 929 C ILE A 154 29.584 18.924 19.146 1.00 29.16 C ATOM 930 O ILE A 154 28.354 19.036 19.204 1.00 25.93 O ATOM 931 CB ILE A 154 31.097 19.406 21.133 1.00 28.95 C ATOM 932 CG1 ILE A 154 31.327 18.914 22.560 1.00 30.02 C ATOM 933 CG2 ILE A 154 30.300 20.712 21.162 1.00 17.91 C ATOM 934 CD1 ILE A 154 32.452 19.617 23.273 1.00 40.22 C ATOM 935 N CYS A 155 30.292 19.304 18.090 1.00 22.97 N ATOM 936 CA CYS A 155 29.688 20.029 16.980 1.00 26.86 C ATOM 937 C CYS A 155 28.842 19.124 16.105 1.00 27.20 C ATOM 938 O CYS A 155 27.834 19.546 15.548 1.00 21.85 O ATOM 939 CB CYS A 155 30.771 20.704 16.130 1.00 46.42 C ATOM 940 SG CYS A 155 31.803 21.872 17.055 1.00 62.56 S ATOM 941 N THR A 156 29.278 17.884 15.964 1.00 26.28 N ATOM 942 CA THR A 156 28.499 16.876 15.274 1.00 27.43 C ATOM 943 C THR A 156 27.156 16.735 15.994 1.00 22.78 C ATOM 944 O THR A 156 26.109 16.695 15.354 1.00 23.07 O ATOM 945 CB THR A 156 29.267 15.525 15.233 1.00 24.67 C ATOM 946 OG1 THR A 156 30.516 15.725 14.573 1.00 32.61 O ATOM 947 CG2 THR A 156 28.499 14.454 14.487 1.00 16.93 C ATOM 948 N VAL A 157 27.196 16.683 17.323 1.00 22.85 N ATOM 949 CA VAL A 157 25.986 16.642 18.135 1.00 19.97 C ATOM 950 C VAL A 157 25.076 17.855 17.938 1.00 20.65 C ATOM 951 O VAL A 157 23.886 17.696 17.714 1.00 23.98 O ATOM 952 CB VAL A 157 26.321 16.492 19.609 1.00 19.03 C ATOM 953 CG1 VAL A 157 25.172 17.006 20.455 1.00 28.71 C ATOM 954 CG2 VAL A 157 26.606 15.037 19.927 1.00 20.93 C ATOM 955 N TRP A 158 25.630 19.061 18.012 1.00 22.27 N ATOM 956 CA TRP A 158 24.857 20.275 17.747 1.00 19.73 C ATOM 957 C TRP A 158 24.307 20.339 16.310 1.00 24.62 C ATOM 958 O TRP A 158 23.186 20.804 16.078 1.00 21.21 O ATOM 959 CB TRP A 158 25.688 21.522 18.080 1.00 18.83 C ATOM 960 CG TRP A 158 25.735 21.824 19.559 1.00 33.40 C ATOM 961 CD1 TRP A 158 26.697 21.433 20.451 1.00 32.62 C ATOM 962 CD2 TRP A 158 24.775 22.574 20.314 1.00 33.09 C ATOM 963 NE1 TRP A 158 26.393 21.890 21.712 1.00 24.67 N ATOM 964 CE2 TRP A 158 25.221 22.592 21.657 1.00 29.13 C ATOM 965 CE3 TRP A 158 23.583 23.231 19.988 1.00 32.10 C ATOM 966 CZ2 TRP A 158 24.520 23.243 22.671 1.00 33.07 C ATOM 967 CZ3 TRP A 158 22.883 23.877 21.001 1.00 41.35 C ATOM 968 CH2 TRP A 158 23.356 23.878 22.329 1.00 33.80 C ATOM 969 N ALA A 159 25.103 19.878 15.345 1.00 29.11 N ATOM 970 CA ALA A 159 24.672 19.775 13.949 1.00 19.78 C ATOM 971 C ALA A 159 23.450 18.876 13.811 1.00 24.84 C ATOM 972 O ALA A 159 22.405 19.309 13.319 1.00 23.96 O ATOM 973 CB ALA A 159 25.780 19.226 13.107 1.00 20.95 C ATOM 974 N ILE A 160 23.601 17.620 14.229 1.00 17.70 N ATOM 975 CA ILE A 160 22.496 16.672 14.219 1.00 21.33 C ATOM 976 C ILE A 160 21.284 17.252 14.906 1.00 26.70 C ATOM 977 O ILE A 160 20.145 17.048 14.479 1.00 26.14 O ATOM 978 CB ILE A 160 22.866 15.354 14.901 1.00 26.99 C ATOM 979 CG1 ILE A 160 23.926 14.627 14.066 1.00 28.62 C ATOM 980 CG2 ILE A 160 21.628 14.493 15.089 1.00 18.16 C ATOM 981 CD1 ILE A 160 24.569 13.445 14.770 1.00 21.61 C ATOM 982 N SER A 161 21.534 17.999 15.968 1.00 24.93 N ATOM 983 CA SER A 161 20.451 18.604 16.729 1.00 26.83 C ATOM 984 C SER A 161 19.682 19.686 15.965 1.00 20.50 C ATOM 985 O SER A 161 18.462 19.649 15.946 1.00 29.11 O ATOM 986 CB SER A 161 20.969 19.129 18.066 1.00 29.32 C ATOM 987 OG SER A 161 21.426 18.054 18.865 1.00 30.79 O ATOM 988 N ALA A 162 20.376 20.642 15.348 1.00 18.91 N ATOM 989 CA ALA A 162 19.706 21.626 14.489 1.00 27.30 C ATOM 990 C ALA A 162 18.953 20.965 13.305 1.00 30.30 C ATOM 991 O ALA A 162 17.845 21.369 12.948 1.00 25.01 O ATOM 992 CB ALA A 162 20.699 22.660 13.991 1.00 16.13 C ATOM 993 N LEU A 163 19.568 19.952 12.704 1.00 23.68 N ATOM 994 CA LEU A 163 18.916 19.143 11.689 1.00 26.16 C ATOM 995 C LEU A 163 17.496 18.688 12.086 1.00 25.27 C ATOM 996 O LEU A 163 16.530 19.025 11.410 1.00 24.44 O ATOM 997 CB LEU A 163 19.773 17.915 11.374 1.00 28.68 C ATOM 998 CG LEU A 163 19.275 17.108 10.180 1.00 20.52 C ATOM 999 CD1 LEU A 163 19.145 18.042 9.002 1.00 14.46 C ATOM 1000 CD2 LEU A 163 20.205 15.952 9.892 1.00 16.80 C ATOM 1001 N VAL A 164 17.380 17.909 13.160 1.00 28.53 N ATOM 1002 CA VAL A 164 16.083 17.364 13.599 1.00 32.39 C ATOM 1003 C VAL A 164 15.200 18.340 14.381 1.00 27.04 C ATOM 1004 O VAL A 164 14.099 17.971 14.803 1.00 32.15 O ATOM 1005 CB VAL A 164 16.229 16.067 14.455 1.00 28.86 C ATOM 1006 CG1 VAL A 164 17.227 15.119 13.825 1.00 20.66 C ATOM 1007 CG2 VAL A 164 16.620 16.396 15.893 1.00 17.30 C ATOM 1008 N SER A 165 15.663 19.573 14.563 1.00 20.24 N ATOM 1009 CA SER A 165 14.873 20.570 15.282 1.00 20.64 C ATOM 1010 C SER A 165 14.560 21.863 14.502 1.00 24.66 C ATOM 1011 O SER A 165 13.401 22.262 14.410 1.00 33.28 O ATOM 1012 CB SER A 165 15.528 20.881 16.624 1.00 27.55 C ATOM 1013 OG SER A 165 16.804 21.453 16.417 1.00 43.75 O ATOM 1014 N PHE A 166 15.572 22.519 13.943 1.00 24.24 N ATOM 1015 CA PHE A 166 15.323 23.676 13.070 1.00 32.73 C ATOM 1016 C PHE A 166 14.622 23.336 11.749 1.00 33.79 C ATOM 1017 O PHE A 166 13.695 24.028 11.325 1.00 26.90 O ATOM 1018 CB PHE A 166 16.621 24.382 12.720 1.00 32.56 C ATOM 1019 CG PHE A 166 17.183 25.175 13.831 1.00 36.86 C ATOM 1020 CD1 PHE A 166 18.557 25.337 13.960 1.00 42.13 C ATOM 1021 CD2 PHE A 166 16.346 25.750 14.760 1.00 27.66 C ATOM 1022 CE1 PHE A 166 19.086 26.083 15.004 1.00 49.22 C ATOM 1023 CE2 PHE A 166 16.855 26.495 15.803 1.00 38.43 C ATOM 1024 CZ PHE A 166 18.226 26.663 15.932 1.00 48.77 C ATOM 1025 N LEU A 167 15.079 22.276 11.095 1.00 29.01 N ATOM 1026 CA LEU A 167 14.688 22.029 9.721 1.00 24.00 C ATOM 1027 C LEU A 167 13.249 21.591 9.475 1.00 24.04 C ATOM 1028 O LEU A 167 12.648 22.020 8.498 1.00 27.98 O ATOM 1029 CB LEU A 167 15.692 21.113 9.028 1.00 28.26 C ATOM 1030 CG LEU A 167 16.711 21.960 8.264 1.00 31.54 C ATOM 1031 CD1 LEU A 167 18.045 21.265 8.175 1.00 25.53 C ATOM 1032 CD2 LEU A 167 16.168 22.307 6.879 1.00 27.18 C ATOM 1033 N PRO A 168 12.687 20.732 10.339 1.00 27.75 N ATOM 1034 CA PRO A 168 11.246 20.464 10.183 1.00 26.79 C ATOM 1035 C PRO A 168 10.353 21.669 10.525 1.00 24.39 C ATOM 1036 O PRO A 168 9.212 21.747 10.063 1.00 20.81 O ATOM 1037 CB PRO A 168 11.005 19.312 11.151 1.00 21.91 C ATOM 1038 CG PRO A 168 12.345 18.633 11.234 1.00 24.33 C ATOM 1039 CD PRO A 168 13.330 19.755 11.226 1.00 23.53 C ATOM 1040 N ILE A 169 10.878 22.608 11.305 1.00 19.04 N ATOM 1041 CA ILE A 169 10.124 23.811 11.606 1.00 20.73 C ATOM 1042 C ILE A 169 10.129 24.783 10.434 1.00 24.70 C ATOM 1043 O ILE A 169 9.094 25.359 10.098 1.00 33.23 O ATOM 1044 CB ILE A 169 10.583 24.482 12.919 1.00 26.19 C ATOM 1045 CG1 ILE A 169 10.250 23.557 14.086 1.00 28.71 C ATOM 1046 CG2 ILE A 169 9.914 25.830 13.106 1.00 17.62 C ATOM 1047 CD1 ILE A 169 9.801 24.266 15.320 1.00 35.25 C ATOM 1048 N MET A 170 11.276 24.956 9.790 1.00 28.27 N ATOM 1049 CA MET A 170 11.323 25.824 8.616 1.00 28.46 C ATOM 1050 C MET A 170 10.593 25.255 7.374 1.00 26.77 C ATOM 1051 O MET A 170 10.160 26.011 6.510 1.00 33.14 O ATOM 1052 CB MET A 170 12.757 26.328 8.324 1.00 27.49 C ATOM 1053 CG MET A 170 13.902 25.370 8.644 1.00 30.20 C ATOM 1054 SD MET A 170 15.522 26.149 8.984 1.00 42.10 S ATOM 1055 CE MET A 170 15.607 27.508 7.825 1.00 23.28 C ATOM 1056 N MET A 171 10.428 23.939 7.298 1.00 22.30 N ATOM 1057 CA MET A 171 9.645 23.330 6.225 1.00 23.82 C ATOM 1058 C MET A 171 8.202 23.080 6.651 1.00 28.63 C ATOM 1059 O MET A 171 7.449 22.401 5.963 1.00 22.06 O ATOM 1060 CB MET A 171 10.278 22.025 5.780 1.00 19.47 C ATOM 1061 CG MET A 171 11.685 22.199 5.237 1.00 28.76 C ATOM 1062 SD MET A 171 12.498 20.601 5.081 1.00 36.21 S ATOM 1063 CE MET A 171 11.485 19.901 3.773 1.00 63.05 C ATOM 1064 N HIS A 172 7.837 23.612 7.808 1.00 23.06 N ATOM 1065 CA HIS A 172 6.469 23.532 8.294 1.00 28.74 C ATOM 1066 C HIS A 172 5.919 22.113 8.461 1.00 26.57 C ATOM 1067 O HIS A 172 4.716 21.909 8.381 1.00 30.69 O ATOM 1068 CB HIS A 172 5.546 24.347 7.390 1.00 20.36 C ATOM 1069 CG HIS A 172 6.039 25.737 7.123 1.00 21.94 C ATOM 1070 ND1 HIS A 172 5.523 26.841 7.757 1.00 24.43 N ATOM 1071 CD2 HIS A 172 6.992 26.193 6.281 1.00 25.54 C ATOM 1072 CE1 HIS A 172 6.149 27.926 7.326 1.00 24.60 C ATOM 1073 NE2 HIS A 172 7.036 27.562 6.426 1.00 25.10 N ATOM 1074 N TRP A 173 6.788 21.148 8.734 1.00 22.96 N ATOM 1075 CA TRP A 173 6.374 19.747 8.827 1.00 24.25 C ATOM 1076 C TRP A 173 5.522 19.491 10.059 1.00 31.27 C ATOM 1077 O TRP A 173 4.900 18.439 10.190 1.00 32.37 O ATOM 1078 CB TRP A 173 7.598 18.834 8.859 1.00 21.12 C ATOM 1079 CG TRP A 173 8.265 18.658 7.535 1.00 23.88 C ATOM 1080 CD1 TRP A 173 8.046 19.387 6.399 1.00 22.56 C ATOM 1081 CD2 TRP A 173 9.286 17.710 7.210 1.00 28.30 C ATOM 1082 NE1 TRP A 173 8.853 18.936 5.388 1.00 23.45 N ATOM 1083 CE2 TRP A 173 9.624 17.905 5.857 1.00 26.74 C ATOM 1084 CE3 TRP A 173 9.943 16.701 7.931 1.00 23.21 C ATOM 1085 CZ2 TRP A 173 10.592 17.133 5.207 1.00 23.76 C ATOM 1086 CZ3 TRP A 173 10.899 15.934 7.278 1.00 26.95 C ATOM 1087 CH2 TRP A 173 11.214 16.154 5.932 1.00 17.99 C ATOM 1088 N TRP A 174 5.489 20.465 10.959 1.00 28.57 N ATOM 1089 CA TRP A 174 4.858 20.284 12.255 1.00 21.85 C ATOM 1090 C TRP A 174 3.386 20.668 12.261 1.00 27.91 C ATOM 1091 O TRP A 174 2.632 20.232 13.134 1.00 26.71 O ATOM 1092 CB TRP A 174 5.591 21.112 13.302 1.00 22.27 C ATOM 1093 CG TRP A 174 5.600 22.570 13.003 1.00 20.96 C ATOM 1094 CD1 TRP A 174 6.434 23.224 12.145 1.00 22.59 C ATOM 1095 CD2 TRP A 174 4.726 23.567 13.549 1.00 19.39 C ATOM 1096 NE1 TRP A 174 6.139 24.568 12.125 1.00 19.11 N ATOM 1097 CE2 TRP A 174 5.097 24.803 12.981 1.00 17.65 C ATOM 1098 CE3 TRP A 174 3.663 23.533 14.456 1.00 20.83 C ATOM 1099 CZ2 TRP A 174 4.453 25.990 13.300 1.00 18.18 C ATOM 1100 CZ3 TRP A 174 3.031 24.717 14.773 1.00 18.72 C ATOM 1101 CH2 TRP A 174 3.426 25.927 14.201 1.00 15.43 C ATOM 1102 N ARG A 175 2.973 21.482 11.293 1.00 29.72 N ATOM 1103 CA ARG A 175 1.633 22.078 11.319 1.00 35.08 C ATOM 1104 C ARG A 175 0.459 21.091 11.156 1.00 35.34 C ATOM 1105 O ARG A 175 0.580 20.058 10.508 1.00 27.63 O ATOM 1106 CB ARG A 175 1.534 23.213 10.302 1.00 19.16 C ATOM 1107 CG ARG A 175 2.477 24.340 10.578 1.00 17.50 C ATOM 1108 CD ARG A 175 2.099 25.549 9.767 1.00 24.78 C ATOM 1109 NE ARG A 175 3.179 26.520 9.644 1.00 18.77 N ATOM 1110 CZ ARG A 175 3.331 27.565 10.448 1.00 25.99 C ATOM 1111 NH1 ARG A 175 2.476 27.774 11.445 1.00 28.26 N ATOM 1112 NH2 ARG A 175 4.339 28.406 10.258 1.00 27.58 N ATOM 1113 N ASP A 176 −0.678 21.425 11.760 1.00 42.01 N ATOM 1114 CA ASP A 176 −1.878 20.602 11.633 1.00 42.19 C ATOM 1115 C ASP A 176 −2.897 21.224 10.674 1.00 35.42 C ATOM 1116 O ASP A 176 −2.731 22.354 10.221 1.00 33.26 O ATOM 1117 CB ASP A 176 −2.504 20.347 13.004 1.00 35.28 C ATOM 1118 CG ASP A 176 −3.238 19.014 13.071 1.00 59.33 C ATOM 1119 OD1 ASP A 176 −3.276 18.278 12.052 1.00 49.89 O ATOM 1120 OD2 ASP A 176 −3.774 18.697 14.156 1.00 63.93 O ATOM 1121 N GLU A 177 −3.939 20.469 10.353 1.00 43.63 N ATOM 1122 CA GLU A 177 −4.968 20.943 9.435 1.00 46.14 C ATOM 1123 C GLU A 177 −6.194 21.532 10.159 1.00 47.04 C ATOM 1124 O GLU A 177 −6.865 22.414 9.620 1.00 47.13 O ATOM 1125 CB GLU A 177 −5.382 19.833 8.460 1.00 48.62 C ATOM 1126 CG GLU A 177 −4.227 19.159 7.707 1.00 53.09 C ATOM 1127 CD GLU A 177 −3.646 20.017 6.585 1.00 79.57 C ATOM 1128 OE1 GLU A 177 −4.037 21.203 6.469 1.00 78.39 O ATOM 1129 OE2 GLU A 177 −2.796 19.504 5.818 1.00 60.84 O ATOM 1130 N ASP A 178 −6.464 21.063 11.381 1.00 51.55 N ATOM 1131 CA ASP A 178 −7.569 21.575 12.229 1.00 58.72 C ATOM 1132 C ASP A 178 −7.781 23.093 12.243 1.00 55.59 C ATOM 1133 O ASP A 178 −6.826 23.869 12.315 1.00 46.01 O ATOM 1134 CB ASP A 178 −7.399 21.117 13.678 1.00 57.10 C ATOM 1135 CG ASP A 178 −7.612 19.631 13.849 1.00 99.36 C ATOM 1136 OD1 ASP A 178 −7.832 18.939 12.830 1.00 105.06 O ATOM 1137 OD2 ASP A 178 −7.557 19.154 15.005 1.00 120.64 O ATOM 1138 N PRO A 179 −9.052 23.518 12.238 1.00 60.41 N ATOM 1139 CA PRO A 179 −9.358 24.952 12.208 1.00 58.74 C ATOM 1140 C PRO A 179 −8.793 25.599 13.467 1.00 50.01 C ATOM 1141 O PRO A 179 −8.323 26.742 13.460 1.00 42.90 O ATOM 1142 CB PRO A 179 −10.896 24.993 12.237 1.00 57.53 C ATOM 1143 CG PRO A 179 −11.353 23.562 12.057 1.00 55.42 C ATOM 1144 CD PRO A 179 −10.240 22.701 12.536 1.00 54.12 C ATOM 1145 N GLN A 180 −8.852 24.845 14.555 1.00 45.56 N ATOM 1146 CA GLN A 180 −8.319 25.297 15.823 1.00 55.89 C ATOM 1147 C GLN A 180 −6.843 25.595 15.639 1.00 47.63 C ATOM 1148 O GLN A 180 −6.390 26.705 15.921 1.00 40.03 O ATOM 1149 CB GLN A 180 −8.538 24.229 16.895 1.00 61.65 C ATOM 1150 CG GLN A 180 −10.007 23.862 17.108 1.00 77.78 C ATOM 1151 CD GLN A 180 −10.753 24.859 17.985 1.00 90.62 C ATOM 1152 OE1 GLN A 180 −10.160 25.516 18.846 1.00 86.25 O ATOM 1153 NE2 GLN A 180 −12.065 24.967 17.775 1.00 91.59 N ATOM 1154 N ALA A 181 −6.103 24.605 15.144 1.00 46.94 N ATOM 1155 CA ALA A 181 −4.696 24.797 14.796 1.00 41.73 C ATOM 1156 C ALA A 181 −4.532 25.994 13.868 1.00 42.87 C ATOM 1157 O ALA A 181 −3.665 26.840 14.085 1.00 30.80 O ATOM 1158 CB ALA A 181 −4.148 23.555 14.134 1.00 40.75 C ATOM 1159 N LEU A 182 −5.383 26.052 12.841 1.00 40.09 N ATOM 1160 CA LEU A 182 −5.315 27.094 11.818 1.00 34.23 C ATOM 1161 C LEU A 182 −5.510 28.517 12.361 1.00 33.37 C ATOM 1162 O LEU A 182 −4.798 29.436 11.967 1.00 33.31 O ATOM 1163 CB LEU A 182 −6.288 26.788 10.675 1.00 29.95 C ATOM 1164 CG LEU A 182 −5.913 25.590 9.792 1.00 35.25 C ATOM 1165 CD1 LEU A 182 −6.829 25.503 8.601 1.00 35.01 C ATOM 1166 CD2 LEU A 182 −4.469 25.685 9.311 1.00 33.15 C ATOM 1167 N LYS A 183 −6.456 28.703 13.273 1.00 37.94 N ATOM 1168 CA LYS A 183 −6.622 30.010 13.901 1.00 40.85 C ATOM 1169 C LYS A 183 −5.400 30.412 14.750 1.00 42.49 C ATOM 1170 O LYS A 183 −5.041 31.586 14.801 1.00 38.70 O ATOM 1171 CB LYS A 183 −7.931 30.056 14.686 1.00 43.62 C ATOM 1172 CG LYS A 183 −9.120 29.663 13.813 1.00 62.64 C ATOM 1173 CD LYS A 183 −10.471 29.994 14.433 1.00 79.17 C ATOM 1174 CE LYS A 183 −11.606 29.477 13.553 1.00 70.40 C ATOM 1175 NZ LYS A 183 −12.944 29.901 14.039 1.00 77.84 N ATOM 1176 N CYS A 184 −4.752 29.438 15.388 1.00 35.78 N ATOM 1177 CA CYS A 184 −3.492 29.683 16.089 1.00 38.43 C ATOM 1178 C CYS A 184 −2.378 30.103 15.126 1.00 35.36 C ATOM 1179 O CYS A 184 −1.464 30.847 15.496 1.00 40.56 O ATOM 1180 CB CYS A 184 −3.047 28.444 16.877 1.00 41.23 C ATOM 1181 SG CYS A 184 −1.881 28.806 18.210 1.00 66.98 S ATOM 1182 N TYR A 185 −2.444 29.617 13.892 1.00 30.80 N ATOM 1183 CA TYR A 185 −1.462 30.018 12.894 1.00 30.68 C ATOM 1184 C TYR A 185 −1.705 31.441 12.397 1.00 39.42 C ATOM 1185 O TYR A 185 −0.758 32.131 12.025 1.00 42.41 O ATOM 1186 CB TYR A 185 −1.393 29.036 11.729 1.00 26.92 C ATOM 1187 CG TYR A 185 −1.090 27.623 12.156 1.00 28.58 C ATOM 1188 CD1 TYR A 185 −0.357 27.374 13.303 1.00 22.63 C ATOM 1189 CD2 TYR A 185 −1.532 26.534 11.407 1.00 32.54 C ATOM 1190 CE1 TYR A 185 −0.075 26.082 13.713 1.00 19.52 C ATOM 1191 CE2 TYR A 185 −1.246 25.235 11.799 1.00 31.49 C ATOM 1192 CZ TYR A 185 −0.515 25.017 12.955 1.00 29.41 C ATOM 1193 OH TYR A 185 −0.222 23.734 13.357 1.00 28.90 O ATOM 1194 N GLN A 186 −2.957 31.896 12.402 1.00 37.20 N ATOM 1195 CA GLN A 186 −3.216 33.301 12.073 1.00 36.36 C ATOM 1196 C GLN A 186 −2.957 34.289 13.224 1.00 39.86 C ATOM 1197 O GLN A 186 −2.350 35.334 13.009 1.00 41.13 O ATOM 1198 CB GLN A 186 −4.586 33.527 11.410 1.00 35.77 C ATOM 1199 CG GLN A 186 −5.634 32.434 11.614 1.00 53.37 C ATOM 1200 CD GLN A 186 −6.921 32.698 10.811 1.00 61.65 C ATOM 1201 OE1 GLN A 186 −6.930 33.507 9.877 1.00 62.63 O ATOM 1202 NE2 GLN A 186 −8.006 32.016 11.180 1.00 51.74 N ATOM 1203 N ASP A 187 −3.386 33.960 14.440 1.00 41.10 N ATOM 1204 CA ASP A 187 −3.095 34.827 15.581 1.00 45.23 C ATOM 1205 C ASP A 187 −1.588 34.866 15.851 1.00 44.68 C ATOM 1206 O ASP A 187 −0.966 33.831 16.110 1.00 42.14 O ATOM 1207 CB ASP A 187 −3.857 34.381 16.837 1.00 39.82 C ATOM 1208 CG ASP A 187 −4.037 35.516 17.864 1.00 51.97 C ATOM 1209 OD1 ASP A 187 −3.359 36.568 17.757 1.00 41.55 O ATOM 1210 OD2 ASP A 187 −4.874 35.348 18.782 1.00 50.39 O ATOM 1211 N PRO A 188 −0.991 36.065 15.769 1.00 39.86 N ATOM 1212 CA PRO A 188 0.424 36.237 16.105 1.00 44.77 C ATOM 1213 C PRO A 188 0.565 36.191 17.614 1.00 43.12 C ATOM 1214 O PRO A 188 1.616 35.826 18.137 1.00 51.55 O ATOM 1215 CB PRO A 188 0.751 37.642 15.588 1.00 31.78 C ATOM 1216 CG PRO A 188 −0.429 38.058 14.773 1.00 40.94 C ATOM 1217 CD PRO A 188 −1.600 37.320 15.318 1.00 37.11 C ATOM 1218 N GLY A 189 −0.512 36.555 18.297 1.00 31.80 N ATOM 1219 CA GLY A 189 −0.549 36.533 19.740 1.00 32.93 C ATOM 1220 C GLY A 189 −0.746 35.139 20.291 1.00 34.14 C ATOM 1221 O GLY A 189 −0.733 34.938 21.501 1.00 45.59 O ATOM 1222 N CYS A 190 −0.945 34.172 19.409 1.00 33.34 N ATOM 1223 CA CYS A 190 −0.975 32.790 19.844 1.00 35.33 C ATOM 1224 C CYS A 190 0.304 32.064 19.432 1.00 36.09 C ATOM 1225 O CYS A 190 0.658 32.000 18.254 1.00 35.20 O ATOM 1226 CB CYS A 190 −2.204 32.068 19.312 1.00 24.66 C ATOM 1227 SG CYS A 190 −2.130 30.297 19.610 1.00 51.09 S ATOM 1228 N CYS A 191 1.008 31.534 20.420 1.00 33.49 N ATOM 1229 CA CYS A 191 2.246 30.827 20.166 1.00 29.17 C ATOM 1230 C CYS A 191 2.179 29.438 20.756 1.00 31.76 C ATOM 1231 O CYS A 191 3.043 29.038 21.533 1.00 37.94 O ATOM 1232 CB CYS A 191 3.443 31.567 20.753 1.00 28.32 C ATOM 1233 SG CYS A 191 4.992 30.845 20.193 1.00 43.49 S ATOM 1234 N ASP A 192 1.142 28.706 20.382 1.00 25.62 N ATOM 1235 CA ASP A 192 0.945 27.364 20.882 1.00 26.72 C ATOM 1236 C ASP A 192 1.509 26.360 19.892 1.00 34.60 C ATOM 1237 O ASP A 192 1.397 26.516 18.668 1.00 32.55 O ATOM 1238 CB ASP A 192 −0.539 27.118 21.156 1.00 39.57 C ATOM 1239 CG ASP A 192 −1.162 28.217 22.038 1.00 67.23 C ATOM 1240 OD1 ASP A 192 −0.404 28.972 22.693 1.00 59.99 O ATOM 1241 OD2 ASP A 192 −2.410 28.332 22.071 1.00 72.48 O ATOM 1242 N PHE A 193 2.149 25.338 20.427 1.00 23.97 N ATOM 1243 CA PHE A 193 2.825 24.378 19.585 1.00 31.53 C ATOM 1244 C PHE A 193 1.842 23.262 19.267 1.00 30.97 C ATOM 1245 O PHE A 193 1.985 22.124 19.735 1.00 29.86 O ATOM 1246 CB PHE A 193 4.116 23.876 20.263 1.00 27.75 C ATOM 1247 CG PHE A 193 5.098 23.245 19.317 1.00 23.98 C ATOM 1248 CD1 PHE A 193 5.236 23.711 18.013 1.00 26.99 C ATOM 1249 CD2 PHE A 193 5.898 22.191 19.735 1.00 23.09 C ATOM 1250 CE1 PHE A 193 6.152 23.120 17.132 1.00 29.76 C ATOM 1251 CE2 PHE A 193 6.812 21.600 18.868 1.00 28.56 C ATOM 1252 CZ PHE A 193 6.943 22.063 17.564 1.00 20.82 C ATOM 1253 N VAL A 194 0.826 23.625 18.484 1.00 28.33 N ATOM 1254 CA VAL A 194 −0.201 22.700 18.009 1.00 28.69 C ATOM 1255 C VAL A 194 0.326 21.980 16.775 1.00 28.32 C ATOM 1256 O VAL A 194 0.437 22.562 15.701 1.00 29.43 O ATOM 1257 CB VAL A 194 −1.497 23.445 17.610 1.00 32.85 C ATOM 1258 CG1 VAL A 194 −2.687 22.506 17.676 1.00 30.79 C ATOM 1259 CG2 VAL A 194 −1.724 24.663 18.494 1.00 31.67 C ATOM 1260 N THR A 195 0.661 20.710 16.918 1.00 26.32 N ATOM 1261 CA THR A 195 1.304 20.015 15.820 1.00 32.61 C ATOM 1262 C THR A 195 0.447 18.854 15.365 1.00 30.73 C ATOM 1263 O THR A 195 −0.520 18.497 16.029 1.00 31.90 O ATOM 1264 CB THR A 195 2.707 19.521 16.218 1.00 37.42 C ATOM 1265 OG1 THR A 195 2.592 18.377 17.073 1.00 35.35 O ATOM 1266 CG2 THR A 195 3.480 20.627 16.949 1.00 29.09 C ATOM 1267 N ASN A 196 0.789 18.275 14.223 1.00 32.68 N ATOM 1268 CA ASN A 196 0.086 17.093 13.761 1.00 31.79 C ATOM 1269 C ASN A 196 0.601 15.854 14.511 1.00 29.85 C ATOM 1270 O ASN A 196 1.699 15.877 15.072 1.00 28.20 O ATOM 1271 CB ASN A 196 0.200 16.972 12.243 1.00 30.04 C ATOM 1272 CG ASN A 196 1.637 16.817 11.765 1.00 26.39 C ATOM 1273 OD1 ASN A 196 2.235 15.761 11.915 1.00 25.28 O ATOM 1274 ND2 ASN A 196 2.177 17.859 11.157 1.00 26.00 N ATOM 1275 N ARG A 197 −0.203 14.796 14.563 1.00 26.11 N ATOM 1276 CA ARG A 197 0.170 13.599 15.322 1.00 24.93 C ATOM 1277 C ARG A 197 1.451 12.929 14.790 1.00 28.75 C ATOM 1278 O ARG A 197 2.294 12.471 15.575 1.00 27.62 O ATOM 1279 CB ARG A 197 −0.986 12.584 15.394 1.00 22.15 C ATOM 1280 CG ARG A 197 −2.313 13.143 15.883 1.00 34.94 C ATOM 1281 CD ARG A 197 −3.333 12.028 16.099 1.00 47.76 C ATOM 1282 NE ARG A 197 −4.677 12.521 16.418 1.00 75.52 N ATOM 1283 CZ ARG A 197 −5.710 11.736 16.733 1.00 93.33 C ATOM 1284 NH1 ARG A 197 −5.561 10.416 16.781 1.00 86.60 N ATOM 1285 NH2 ARG A 197 −6.897 12.266 17.008 1.00 91.35 N ATOM 1286 N ALA A 198 1.593 12.870 13.464 1.00 23.92 N ATOM 1287 CA ALA A 198 2.799 12.314 12.849 1.00 29.85 C ATOM 1288 C ALA A 198 4.050 12.976 13.422 1.00 29.84 C ATOM 1289 O ALA A 198 4.938 12.307 13.933 1.00 27.52 O ATOM 1290 CB ALA A 198 2.766 12.479 11.335 1.00 24.41 C ATOM 1291 N TYR A 199 4.104 14.298 13.333 1.00 26.70 N ATOM 1292 CA TYR A 199 5.239 15.047 13.820 1.00 23.03 C ATOM 1293 C TYR A 199 5.431 14.850 15.317 1.00 28.75 C ATOM 1294 O TYR A 199 6.537 14.554 15.792 1.00 28.17 O ATOM 1295 CB TYR A 199 5.081 16.534 13.510 1.00 23.59 C ATOM 1296 CG TYR A 199 6.165 17.361 14.150 1.00 26.12 C ATOM 1297 CD1 TYR A 199 7.386 17.563 13.513 1.00 25.09 C ATOM 1298 CD2 TYR A 199 5.984 17.906 15.413 1.00 26.43 C ATOM 1299 CE1 TYR A 199 8.382 18.308 14.109 1.00 23.55 C ATOM 1300 CE2 TYR A 199 6.969 18.651 16.019 1.00 27.78 C ATOM 1301 CZ TYR A 199 8.167 18.851 15.367 1.00 23.70 C ATOM 1302 OH TYR A 199 9.145 19.596 15.987 1.00 21.58 O ATOM 1303 N ALA A 200 4.352 15.019 16.066 1.00 29.99 N ATOM 1304 CA ALA A 200 4.434 14.921 17.509 1.00 24.14 C ATOM 1305 C ALA A 200 5.115 13.617 17.940 1.00 26.61 C ATOM 1306 O ALA A 200 6.018 13.630 18.761 1.00 29.85 O ATOM 1307 CB ALA A 200 3.062 15.048 18.120 1.00 24.34 C ATOM 1308 N ILE A 201 4.690 12.492 17.383 1.00 25.04 N ATOM 1309 CA ILE A 201 5.314 11.217 17.729 1.00 25.73 C ATOM 1310 C ILE A 201 6.763 11.089 17.234 1.00 33.55 C ATOM 1311 O ILE A 201 7.639 10.653 17.968 1.00 31.35 O ATOM 1312 CB ILE A 201 4.506 10.037 17.182 1.00 34.72 C ATOM 1313 CG1 ILE A 201 3.220 9.869 18.001 1.00 28.60 C ATOM 1314 CG2 ILE A 201 5.369 8.757 17.161 1.00 18.19 C ATOM 1315 CD1 ILE A 201 2.202 8.978 17.341 1.00 28.71 C ATOM 1316 N ALA A 202 7.010 11.470 15.987 1.00 31.95 N ATOM 1317 CA ALA A 202 8.322 11.296 15.391 1.00 29.74 C ATOM 1318 C ALA A 202 9.380 12.173 16.053 1.00 30.66 C ATOM 1319 O ALA A 202 10.459 11.693 16.408 1.00 28.11 O ATOM 1320 CB ALA A 202 8.270 11.547 13.872 1.00 26.00 C ATOM 1321 N SER A 203 9.078 13.455 16.223 1.00 28.64 N ATOM 1322 CA SER A 203 10.065 14.372 16.786 1.00 30.99 C ATOM 1323 C SER A 203 10.384 14.005 18.234 1.00 30.08 C ATOM 1324 O SER A 203 11.432 14.360 18.756 1.00 26.38 O ATOM 1325 CB SER A 203 9.584 15.815 16.699 1.00 29.18 C ATOM 1326 OG SER A 203 8.628 16.085 17.698 1.00 26.85 O ATOM 1327 N SER A 204 9.470 13.280 18.864 1.00 26.34 N ATOM 1328 CA SER A 204 9.640 12.848 20.237 1.00 27.24 C ATOM 1329 C SER A 204 10.467 11.569 20.339 1.00 28.35 C ATOM 1330 O SER A 204 11.358 11.459 21.174 1.00 28.24 O ATOM 1331 CB SER A 204 8.274 12.653 20.883 1.00 27.86 C ATOM 1332 OG SER A 204 7.561 13.876 20.851 1.00 31.39 O ATOM 1333 N ILE A 205 10.155 10.595 19.497 1.00 29.98 N ATOM 1334 CA ILE A 205 10.971 9.401 19.383 1.00 29.38 C ATOM 1335 C ILE A 205 12.412 9.795 19.063 1.00 36.57 C ATOM 1336 O ILE A 205 13.364 9.237 19.617 1.00 34.55 O ATOM 1337 CB ILE A 205 10.416 8.480 18.282 1.00 37.14 C ATOM 1338 CG1 ILE A 205 9.277 7.632 18.843 1.00 38.59 C ATOM 1339 CG2 ILE A 205 11.499 7.575 17.701 1.00 31.15 C ATOM 1340 CD1 ILE A 205 8.444 6.946 17.772 1.00 32.70 C ATOM 1341 N ILE A 206 12.557 10.790 18.193 1.00 31.89 N ATOM 1342 CA ILE A 206 13.858 11.160 17.642 1.00 31.40 C ATOM 1343 C ILE A 206 14.680 12.156 18.468 1.00 32.64 C ATOM 1344 O ILE A 206 15.909 12.099 18.440 1.00 37.42 O ATOM 1345 CB ILE A 206 13.712 11.647 16.173 1.00 32.59 C ATOM 1346 CG1 ILE A 206 13.859 10.460 15.222 1.00 29.53 C ATOM 1347 CG2 ILE A 206 14.721 12.747 15.838 1.00 28.85 C ATOM 1348 CD1 ILE A 206 12.984 10.556 14.006 1.00 34.69 C ATOM 1349 N SER A 207 14.020 13.063 19.188 1.00 27.31 N ATOM 1350 CA SER A 207 14.741 14.032 20.012 1.00 25.97 C ATOM 1351 C SER A 207 14.973 13.501 21.409 1.00 25.69 C ATOM 1352 O SER A 207 15.924 13.890 22.076 1.00 33.19 O ATOM 1353 CB SER A 207 13.991 15.363 20.110 1.00 27.32 C ATOM 1354 OG SER A 207 13.965 16.065 18.873 1.00 30.81 O ATOM 1355 N PHE A 208 14.109 12.603 21.857 1.00 27.94 N ATOM 1356 CA PHE A 208 14.063 12.287 23.280 1.00 24.68 C ATOM 1357 C PHE A 208 14.166 10.806 23.635 1.00 27.29 C ATOM 1358 O PHE A 208 15.117 10.399 24.302 1.00 36.16 O ATOM 1359 CB PHE A 208 12.819 12.911 23.937 1.00 24.28 C ATOM 1360 CG PHE A 208 12.767 12.713 25.418 1.00 26.55 C ATOM 1361 CD1 PHE A 208 13.546 13.495 26.268 1.00 32.55 C ATOM 1362 CD2 PHE A 208 11.987 11.713 25.966 1.00 25.08 C ATOM 1363 CE1 PHE A 208 13.528 13.283 27.642 1.00 20.70 C ATOM 1364 CE2 PHE A 208 11.960 11.513 27.319 1.00 21.33 C ATOM 1365 CZ PHE A 208 12.732 12.295 28.155 1.00 20.46 C ATOM 1366 N TYR A 209 13.193 10.009 23.202 1.00 30.38 N ATOM 1367 CA TYR A 209 13.093 8.606 23.619 1.00 34.21 C ATOM 1368 C TYR A 209 14.255 7.709 23.177 1.00 32.23 C ATOM 1369 O TYR A 209 14.728 6.880 23.945 1.00 34.31 O ATOM 1370 CB TYR A 209 11.745 7.993 23.199 1.00 31.12 C ATOM 1371 CG TYR A 209 10.569 8.498 24.004 1.00 32.22 C ATOM 1372 CD1 TYR A 209 9.618 9.328 23.431 1.00 33.48 C ATOM 1373 CD2 TYR A 209 10.417 8.156 25.344 1.00 37.94 C ATOM 1374 CE1 TYR A 209 8.537 9.796 24.162 1.00 31.62 C ATOM 1375 CE2 TYR A 209 9.338 8.619 26.083 1.00 36.43 C ATOM 1376 CZ TYR A 209 8.402 9.441 25.484 1.00 39.13 C ATOM 1377 OH TYR A 209 7.329 9.914 26.202 1.00 43.68 O ATOM 1378 N ILE A 210 14.719 7.851 21.946 1.00 32.61 N ATOM 1379 CA ILE A 210 15.854 7.032 21.531 1.00 34.83 C ATOM 1380 C ILE A 210 17.142 7.413 22.261 1.00 26.35 C ATOM 1381 O ILE A 210 17.748 6.574 22.912 1.00 31.51 O ATOM 1382 CB ILE A 210 16.035 6.989 20.003 1.00 33.32 C ATOM 1383 CG1 ILE A 210 14.942 6.116 19.385 1.00 28.85 C ATOM 1384 CG2 ILE A 210 17.406 6.433 19.634 1.00 33.18 C ATOM 1385 CD1 ILE A 210 14.731 6.380 17.910 1.00 32.45 C ATOM 1386 N PRO A 211 17.556 8.682 22.175 1.00 27.02 N ATOM 1387 CA PRO A 211 18.757 9.082 22.921 1.00 29.20 C ATOM 1388 C PRO A 211 18.639 8.675 24.390 1.00 38.43 C ATOM 1389 O PRO A 211 19.628 8.268 24.993 1.00 40.54 O ATOM 1390 CB PRO A 211 18.755 10.610 22.813 1.00 27.67 C ATOM 1391 CG PRO A 211 17.932 10.912 21.620 1.00 35.57 C ATOM 1392 CD PRO A 211 16.933 9.805 21.459 1.00 26.23 C ATOM 1393 N LEU A 212 17.436 8.777 24.954 1.00 33.08 N ATOM 1394 CA LEU A 212 17.196 8.355 26.332 1.00 29.10 C ATOM 1395 C LEU A 212 17.441 6.860 26.560 1.00 33.70 C ATOM 1396 O LEU A 212 18.214 6.481 27.437 1.00 38.29 O ATOM 1397 CB LEU A 212 15.779 8.717 26.772 1.00 30.14 C ATOM 1398 CG LEU A 212 15.534 8.587 28.279 1.00 31.90 C ATOM 1399 CD1 LEU A 212 16.223 9.720 29.057 1.00 21.99 C ATOM 1400 CD2 LEU A 212 14.060 8.573 28.556 1.00 26.71 C ATOM 1401 N LEU A 213 16.776 6.020 25.775 1.00 34.42 N ATOM 1402 CA LEU A 213 16.964 4.576 25.849 1.00 33.11 C ATOM 1403 C LEU A 213 18.431 4.178 25.718 1.00 34.57 C ATOM 1404 O LEU A 213 18.883 3.244 26.371 1.00 29.68 O ATOM 1405 CB LEU A 213 16.140 3.881 24.768 1.00 32.56 C ATOM 1406 CG LEU A 213 14.635 4.014 24.996 1.00 48.49 C ATOM 1407 CD1 LEU A 213 13.857 3.555 23.778 1.00 45.04 C ATOM 1408 CD2 LEU A 213 14.206 3.240 26.235 1.00 40.44 C ATOM 1409 N ILE A 214 19.169 4.889 24.867 1.00 31.91 N ATOM 1410 CA ILE A 214 20.591 4.628 24.694 1.00 31.18 C ATOM 1411 C ILE A 214 21.356 5.016 25.943 1.00 38.97 C ATOM 1412 O ILE A 214 22.099 4.212 26.507 1.00 41.86 O ATOM 1413 CB ILE A 214 21.180 5.426 23.529 1.00 35.18 C ATOM 1414 CG1 ILE A 214 20.702 4.856 22.204 1.00 31.13 C ATOM 1415 CG2 ILE A 214 22.714 5.419 23.584 1.00 30.25 C ATOM 1416 CD1 ILE A 214 21.109 5.689 21.046 1.00 32.06 C ATOM 1417 N MET A 215 21.171 6.258 26.374 1.00 31.21 N ATOM 1418 CA MET A 215 21.867 6.764 27.546 1.00 34.92 C ATOM 1419 C MET A 215 21.683 5.873 28.778 1.00 40.82 C ATOM 1420 O MET A 215 22.620 5.676 29.545 1.00 36.54 O ATOM 1421 CB MET A 215 21.417 8.184 27.867 1.00 35.42 C ATOM 1422 CG MET A 215 22.183 8.813 29.015 1.00 33.32 C ATOM 1423 SD MET A 215 21.246 10.158 29.733 1.00 48.20 S ATOM 1424 CE MET A 215 19.950 9.220 30.541 1.00 39.49 C ATOM 1425 N ILE A 216 20.475 5.346 28.965 1.00 36.27 N ATOM 1426 CA ILE A 216 20.196 4.476 30.094 1.00 36.52 C ATOM 1427 C ILE A 216 20.876 3.127 29.945 1.00 40.79 C ATOM 1428 O ILE A 216 21.622 2.707 30.828 1.00 45.81 O ATOM 1429 CB ILE A 216 18.689 4.261 30.313 1.00 45.28 C ATOM 1430 CG1 ILE A 216 18.121 5.400 31.160 1.00 39.15 C ATOM 1431 CG2 ILE A 216 18.432 2.908 30.991 1.00 26.27 C ATOM 1432 CD1 ILE A 216 16.675 5.723 30.841 1.00 35.73 C ATOM 1433 N PHE A 217 20.620 2.443 28.839 1.00 31.07 N ATOM 1434 CA PHE A 217 21.259 1.164 28.615 1.00 32.64 C ATOM 1435 C PHE A 217 22.775 1.272 28.782 1.00 44.70 C ATOM 1436 O PHE A 217 23.409 0.369 29.322 1.00 46.59 O ATOM 1437 CB PHE A 217 20.921 0.605 27.239 1.00 42.52 C ATOM 1438 CG PHE A 217 21.672 −0.645 26.908 1.00 59.40 C ATOM 1439 CD1 PHE A 217 21.379 −1.832 27.557 1.00 66.77 C ATOM 1440 CD2 PHE A 217 22.691 −0.633 25.965 1.00 73.28 C ATOM 1441 CE1 PHE A 217 22.079 −2.993 27.264 1.00 79.21 C ATOM 1442 CE2 PHE A 217 23.397 −1.792 25.661 1.00 68.73 C ATOM 1443 CZ PHE A 217 23.090 −2.972 26.313 1.00 75.53 C ATOM 1444 N VAL A 218 23.357 2.380 28.334 1.00 42.28 N ATOM 1445 CA VAL A 218 24.801 2.574 28.456 1.00 41.92 C ATOM 1446 C VAL A 218 25.236 2.913 29.888 1.00 40.46 C ATOM 1447 O VAL A 218 26.172 2.316 30.415 1.00 39.77 O ATOM 1448 CB VAL A 218 25.331 3.630 27.452 1.00 43.63 C ATOM 1449 CG1 VAL A 218 26.761 4.039 27.784 1.00 33.36 C ATOM 1450 CG2 VAL A 218 25.258 3.085 26.035 1.00 30.46 C ATOM 1451 N ALA A 219 24.554 3.863 30.515 1.00 42.47 N ATOM 1452 CA ALA A 219 24.829 4.206 31.905 1.00 39.30 C ATOM 1453 C ALA A 219 24.733 2.994 32.828 1.00 40.43 C ATOM 1454 O ALA A 219 25.494 2.884 33.786 1.00 42.68 O ATOM 1455 CB ALA A 219 23.891 5.303 32.379 1.00 35.20 C ATOM 1456 N LEU A 220 23.800 2.090 32.547 1.00 37.44 N ATOM 1457 CA LEU A 220 23.673 0.880 33.347 1.00 42.28 C ATOM 1458 C LEU A 220 24.886 −0.045 33.176 1.00 46.75 C ATOM 1459 O LEU A 220 25.362 −0.637 34.148 1.00 54.13 O ATOM 1460 CB LEU A 220 22.358 0.147 33.049 1.00 37.79 C ATOM 1461 CG LEU A 220 21.096 0.829 33.605 1.00 56.15 C ATOM 1462 CD1 LEU A 220 19.930 −0.151 33.701 1.00 42.10 C ATOM 1463 CD2 LEU A 220 21.334 1.514 34.965 1.00 23.99 C ATOM 1464 N ARG A 221 25.375 −0.162 31.940 1.00 34.06 N ATOM 1465 CA ARG A 221 26.633 −0.857 31.645 1.00 47.01 C ATOM 1466 C ARG A 221 27.847 −0.270 32.381 1.00 44.19 C ATOM 1467 O ARG A 221 28.697 −1.004 32.875 1.00 49.15 O ATOM 1468 CB ARG A 221 26.922 −0.852 30.135 1.00 51.35 C ATOM 1469 CG ARG A 221 26.069 −1.807 29.295 1.00 47.59 C ATOM 1470 CD ARG A 221 25.852 −3.157 29.978 1.00 60.46 C ATOM 1471 NE ARG A 221 27.105 −3.818 30.337 1.00 81.42 N ATOM 1472 CZ ARG A 221 27.181 −4.943 31.044 1.00 86.87 C ATOM 1473 NH1 ARG A 221 26.071 −5.536 31.465 1.00 84.36 N ATOM 1474 NH2 ARG A 221 28.366 −5.475 31.329 1.00 94.79 N ATOM 1475 N VAL A 222 27.926 1.056 32.431 1.00 50.12 N ATOM 1476 CA VAL A 222 28.997 1.765 33.130 1.00 46.09 C ATOM 1477 C VAL A 222 28.925 1.534 34.639 1.00 53.14 C ATOM 1478 O VAL A 222 29.954 1.329 35.288 1.00 53.44 O ATOM 1479 CB VAL A 222 28.958 3.282 32.818 1.00 35.48 C ATOM 1480 CG1 VAL A 222 29.921 4.055 33.704 1.00 33.70 C ATOM 1481 CG2 VAL A 222 29.276 3.522 31.364 1.00 37.85 C ATOM 1482 N TYR A 223 27.709 1.566 35.187 1.00 47.31 N ATOM 1483 CA TYR A 223 27.472 1.227 36.591 1.00 56.01 C ATOM 1484 C TYR A 223 27.973 −0.187 36.919 1.00 61.05 C ATOM 1485 O TYR A 223 28.700 −0.388 37.895 1.00 58.67 O ATOM 1486 CB TYR A 223 25.980 1.342 36.915 1.00 55.83 C ATOM 1487 CG TYR A 223 25.614 1.018 38.353 1.00 76.27 C ATOM 1488 CD1 TYR A 223 25.703 1.986 39.348 1.00 78.06 C ATOM 1489 CD2 TYR A 223 25.168 −0.251 38.711 1.00 68.54 C ATOM 1490 CE1 TYR A 223 25.367 1.700 40.656 1.00 81.59 C ATOM 1491 CE2 TYR A 223 24.834 −0.548 40.019 1.00 67.78 C ATOM 1492 CZ TYR A 223 24.934 0.432 40.987 1.00 89.61 C ATOM 1493 OH TYR A 223 24.600 0.148 42.292 1.00 103.52 O ATOM 1494 N ARG A 224 27.586 −1.144 36.074 1.00 47.11 N ATOM 1495 CA ARG A 224 27.962 −2.554 36.188 1.00 52.64 C ATOM 1496 C ARG A 224 29.468 −2.783 36.074 1.00 58.78 C ATOM 1497 O ARG A 224 29.998 −3.746 36.604 1.00 61.77 O ATOM 1498 CB ARG A 224 27.249 −3.357 35.096 1.00 53.18 C ATOM 1499 CG ARG A 224 27.122 −4.847 35.365 1.00 67.01 C ATOM 1500 CD ARG A 224 28.441 −5.575 35.182 1.00 73.85 C ATOM 1501 NE ARG A 224 28.354 −6.976 35.590 1.00 92.74 N ATOM 1502 CZ ARG A 224 28.427 −7.403 36.849 1.00 89.22 C ATOM 1503 NH1 ARG A 224 28.595 −6.535 37.836 1.00 99.73 N ATOM 1504 NH2 ARG A 224 28.334 −8.700 37.125 1.00 81.42 N ATOM 1505 N GLU A 225 30.149 −1.907 35.356 1.00 62.29 N ATOM 1506 CA GLU A 225 31.599 −1.961 35.232 1.00 61.05 C ATOM 1507 C GLU A 225 32.295 −1.296 36.416 1.00 67.83 C ATOM 1508 O GLU A 225 33.271 −1.822 36.938 1.00 78.23 O ATOM 1509 CB GLU A 225 32.044 −1.305 33.923 1.00 59.05 C ATOM 1510 CG GLU A 225 32.030 −2.247 32.723 1.00 75.98 C ATOM 1511 CD GLU A 225 33.138 −3.290 32.779 1.00 84.71 C ATOM 1512 OE1 GLU A 225 33.760 −3.454 33.850 1.00 86.02 O ATOM 1513 OE2 GLU A 225 33.389 −3.944 31.746 1.00 89.53 O ATOM 1514 N ALA A 226 31.790 −0.140 36.836 1.00 61.93 N ATOM 1515 CA ALA A 226 32.343 0.561 37.986 1.00 62.44 C ATOM 1516 C ALA A 226 32.159 −0.269 39.250 1.00 75.28 C ATOM 1517 O ALA A 226 32.954 −0.178 40.181 1.00 86.17 O ATOM 1518 CB ALA A 226 31.690 1.927 38.145 1.00 54.77 C ATOM 1519 N LYS A 227 31.111 −1.084 39.273 1.00 70.13 N ATOM 1520 CA LYS A 227 30.803 −1.915 40.432 1.00 72.99 C ATOM 1521 C LYS A 227 31.701 −3.143 40.486 1.00 69.03 C ATOM 1522 O LYS A 227 32.511 −3.293 41.402 1.00 79.39 O ATOM 1523 CB LYS A 227 29.339 −2.355 40.390 1.00 86.73 C ATOM 1524 CG LYS A 227 28.929 −3.270 41.531 1.00 94.76 C ATOM 1525 CD LYS A 227 27.717 −4.110 41.156 1.00 88.99 C ATOM 1526 CE LYS A 227 27.297 −5.013 42.307 1.00 116.52 C ATOM 1527 NZ LYS A 227 28.421 −5.862 42.804 1.00 112.93 N ATOM 1528 N GLU A 228 31.524 −4.001 39.479 1.00 64.08 N ATOM 1529 CA GLU A 228 32.320 −5.206 39.202 1.00 74.72 C ATOM 1530 C GLU A 228 33.802 −4.920 39.309 1.00 76.43 C ATOM 1531 O GLU A 228 34.637 −5.814 39.219 1.00 70.99 O ATOM 1532 CB GLU A 228 32.022 −5.674 37.771 1.00 71.15 C ATOM 1533 CG GLU A 228 32.402 −7.103 37.426 1.00 63.61 C ATOM 1534 CD GLU A 228 32.020 −7.477 35.983 1.00 104.77 C ATOM 1535 OE1 GLU A 228 32.297 −6.678 35.056 1.00 84.00 O ATOM 1536 OE2 GLU A 228 31.442 −8.572 35.776 1.00 107.16 O ATOM 1537 N GLN A 229 34.108 −3.648 39.501 1.00 83.37 N ATOM 1538 CA GLN A 229 35.464 −3.142 39.518 1.00 80.99 C ATOM 1539 C GLN A 229 35.900 −2.898 40.953 1.00 90.06 C ATOM 1540 O GLN A 229 37.006 −3.260 41.348 1.00 104.26 O ATOM 1541 CB GLN A 229 35.478 −1.815 38.775 1.00 84.09 C ATOM 1542 CG GLN A 229 36.733 −1.509 38.015 1.00 76.29 C ATOM 1543 CD GLN A 229 36.716 −0.099 37.472 1.00 79.45 C ATOM 1544 OE1 GLN A 229 37.218 0.163 36.379 1.00 80.07 O ATOM 1545 NE2 GLN A 229 36.122 0.822 38.230 1.00 83.76 N ATOM 1546 N ILE A 230 35.011 −2.271 41.721 1.00 94.97 N ATOM 1547 CA ILE A 230 35.277 −1.834 43.087 1.00 91.78 C ATOM 1548 C ILE A 230 34.317 −0.697 43.378 1.00 77.23 C ATOM 1549 O ILE A 230 33.122 −0.909 43.540 1.00 88.60 O ATOM 1550 CB ILE A 230 36.710 −1.294 43.254 1.00 103.06 C ATOM 1551 CG1 ILE A 230 36.923 −0.751 44.672 1.00 103.08 C ATOM 1552 CG2 ILE A 230 36.993 −0.198 42.227 1.00 94.49 C ATOM 1553 CD1 ILE A 230 36.454 0.687 44.868 1.00 85.77 C ATOM 1554 N ARG A 267 38.234 7.999 43.858 1.00 98.55 N ATOM 1555 CA ARG A 267 37.413 9.201 43.878 1.00 102.83 C ATOM 1556 C ARG A 267 36.747 9.309 42.517 1.00 96.59 C ATOM 1557 O ARG A 267 35.927 10.196 42.272 1.00 87.82 O ATOM 1558 CB ARG A 267 38.268 10.441 44.138 1.00 111.38 C ATOM 1559 CG ARG A 267 38.820 10.543 45.551 1.00 124.33 C ATOM 1560 CD ARG A 267 37.745 10.951 46.554 1.00 126.95 C ATOM 1561 NE ARG A 267 38.293 11.114 47.900 1.00 138.98 N ATOM 1562 CZ ARG A 267 37.607 11.567 48.946 1.00 131.72 C ATOM 1563 NH1 ARG A 267 36.332 11.909 48.814 1.00 114.09 N ATOM 1564 NH2 ARG A 267 38.199 11.679 50.127 1.00 134.30 N ATOM 1565 N GLU A 268 37.125 8.390 41.635 1.00 93.11 N ATOM 1566 CA GLU A 268 36.558 8.301 40.297 1.00 77.06 C ATOM 1567 C GLU A 268 35.093 7.881 40.351 1.00 74.27 C ATOM 1568 O GLU A 268 34.281 8.325 39.544 1.00 69.69 O ATOM 1569 CB GLU A 268 37.352 7.301 39.461 1.00 92.14 C ATOM 1570 CG GLU A 268 38.856 7.545 39.463 1.00 122.45 C ATOM 1571 CD GLU A 268 39.259 8.762 38.645 1.00 134.93 C ATOM 1572 OE1 GLU A 268 38.446 9.216 37.809 1.00 132.98 O ATOM 1573 OE2 GLU A 268 40.391 9.259 38.835 1.00 135.31 O ATOM 1574 N HIS A 269 34.758 7.022 41.307 1.00 80.89 N ATOM 1575 CA HIS A 269 33.372 6.602 41.503 1.00 69.65 C ATOM 1576 C HIS A 269 32.517 7.752 42.013 1.00 58.87 C ATOM 1577 O HIS A 269 31.298 7.741 41.869 1.00 64.21 O ATOM 1578 CB HIS A 269 33.297 5.407 42.454 1.00 64.13 C ATOM 1579 CG HIS A 269 33.790 4.128 41.845 1.00 85.61 C ATOM 1580 ND1 HIS A 269 33.376 2.892 42.276 1.00 87.41 N ATOM 1581 CD2 HIS A 269 34.648 3.911 40.818 1.00 91.53 C ATOM 1582 CE1 HIS A 269 33.974 1.955 41.550 1.00 84.25 C ATOM 1583 NE2 HIS A 269 34.743 2.547 40.659 1.00 82.20 N ATOM 1584 N LYS A 270 33.161 8.755 42.594 1.00 58.96 N ATOM 1585 CA LYS A 270 32.440 9.928 43.065 1.00 72.45 C ATOM 1586 C LYS A 270 32.155 10.879 41.904 1.00 71.67 C ATOM 1587 O LYS A 270 31.130 11.563 41.885 1.00 67.37 O ATOM 1588 CB LYS A 270 33.214 10.607 44.195 1.00 71.70 C ATOM 1589 CG LYS A 270 33.427 9.669 45.379 1.00 98.25 C ATOM 1590 CD LYS A 270 34.450 10.186 46.379 1.00 125.30 C ATOM 1591 CE LYS A 270 34.709 9.159 47.481 1.00 120.65 C ATOM 1592 NZ LYS A 270 33.469 8.790 48.224 1.00 123.08 N ATOM 1593 N ALA A 271 33.057 10.899 40.928 1.00 59.98 N ATOM 1594 CA ALA A 271 32.836 11.650 39.705 1.00 48.84 C ATOM 1595 C ALA A 271 31.776 10.957 38.847 1.00 54.12 C ATOM 1596 O ALA A 271 30.956 11.612 38.197 1.00 48.88 O ATOM 1597 CB ALA A 271 34.127 11.795 38.943 1.00 49.40 C ATOM 1598 N LEU A 272 31.797 9.628 38.853 1.00 44.38 N ATOM 1599 CA LEU A 272 30.792 8.838 38.148 1.00 47.82 C ATOM 1600 C LEU A 272 29.418 8.934 38.803 1.00 51.17 C ATOM 1601 O LEU A 272 28.393 8.820 38.132 1.00 44.10 O ATOM 1602 CB LEU A 272 31.208 7.368 38.070 1.00 48.29 C ATOM 1603 CG LEU A 272 32.341 7.038 37.102 1.00 45.28 C ATOM 1604 CD1 LEU A 272 32.517 5.544 37.033 1.00 41.86 C ATOM 1605 CD2 LEU A 272 32.063 7.608 35.723 1.00 31.56 C ATOM 1606 N LYS A 273 29.388 9.128 40.115 1.00 56.57 N ATOM 1607 CA LYS A 273 28.107 9.180 40.799 1.00 53.05 C ATOM 1608 C LYS A 273 27.394 10.489 40.469 1.00 49.59 C ATOM 1609 O LYS A 273 26.170 10.551 40.432 1.00 42.94 O ATOM 1610 CB LYS A 273 28.273 9.016 42.308 1.00 57.78 C ATOM 1611 CG LYS A 273 27.117 8.254 42.946 1.00 77.19 C ATOM 1612 CD LYS A 273 26.644 8.886 44.253 1.00 78.11 C ATOM 1613 CE LYS A 273 25.549 8.044 44.883 1.00 68.84 C ATOM 1614 NZ LYS A 273 24.992 8.671 46.102 1.00 86.94 N ATOM 1615 N THR A 274 28.177 11.531 40.222 1.00 50.27 N ATOM 1616 CA THR A 274 27.635 12.822 39.838 1.00 45.95 C ATOM 1617 C THR A 274 27.096 12.772 38.408 1.00 41.97 C ATOM 1618 O THR A 274 26.033 13.322 38.116 1.00 37.18 O ATOM 1619 CB THR A 274 28.700 13.922 39.965 1.00 35.46 C ATOM 1620 OG1 THR A 274 29.238 13.902 41.287 1.00 50.74 O ATOM 1621 CG2 THR A 274 28.097 15.291 39.703 1.00 41.95 C ATOM 1622 N LEU A 275 27.834 12.114 37.520 1.00 37.39 N ATOM 1623 CA LEU A 275 27.377 11.932 36.151 1.00 36.72 C ATOM 1624 C LEU A 275 26.046 11.190 36.155 1.00 37.97 C ATOM 1625 O LEU A 275 25.127 11.542 35.417 1.00 28.54 O ATOM 1626 CB LEU A 275 28.410 11.176 35.316 1.00 28.78 C ATOM 1627 CG LEU A 275 29.706 11.951 35.073 1.00 42.27 C ATOM 1628 CD1 LEU A 275 30.639 11.206 34.109 1.00 42.12 C ATOM 1629 CD2 LEU A 275 29.411 13.359 34.555 1.00 33.72 C ATOM 1630 N GLY A 276 25.953 10.172 37.004 1.00 38.06 N ATOM 1631 CA GLY A 276 24.721 9.433 37.193 1.00 35.97 C ATOM 1632 C GLY A 276 23.586 10.296 37.728 1.00 37.74 C ATOM 1633 O GLY A 276 22.452 10.179 37.275 1.00 35.84 O ATOM 1634 N ILE A 277 23.884 11.170 38.685 1.00 37.08 N ATOM 1635 CA ILE A 277 22.875 12.078 39.227 1.00 32.35 C ATOM 1636 C ILE A 277 22.378 13.051 38.160 1.00 31.83 C ATOM 1637 O ILE A 277 21.185 13.302 38.059 1.00 32.48 O ATOM 1638 CB ILE A 277 23.406 12.852 40.462 1.00 38.79 C ATOM 1639 CG1 ILE A 277 23.544 11.910 41.660 1.00 28.85 C ATOM 1640 CG2 ILE A 277 22.498 14.025 40.826 1.00 22.70 C ATOM 1641 CD1 ILE A 277 24.625 12.318 42.636 1.00 46.73 C ATOM 1642 N ILE A 278 23.296 13.583 37.358 1.00 36.24 N ATOM 1643 CA ILE A 278 22.942 14.483 36.258 1.00 35.99 C ATOM 1644 C ILE A 278 21.962 13.837 35.265 1.00 39.36 C ATOM 1645 O ILE A 278 20.994 14.465 34.830 1.00 30.79 O ATOM 1646 CB ILE A 278 24.206 14.948 35.513 1.00 36.39 C ATOM 1647 CG1 ILE A 278 25.039 15.846 36.419 1.00 51.94 C ATOM 1648 CG2 ILE A 278 23.850 15.738 34.290 1.00 36.91 C ATOM 1649 CD1 ILE A 278 24.463 17.221 36.562 1.00 45.67 C ATOM 1650 N MET A 279 22.217 12.576 34.925 1.00 40.29 N ATOM 1651 CA MET A 279 21.408 11.852 33.952 1.00 34.57 C ATOM 1652 C MET A 279 20.055 11.448 34.522 1.00 34.43 C ATOM 1653 O MET A 279 19.051 11.448 33.813 1.00 32.79 O ATOM 1654 CB MET A 279 22.148 10.609 33.453 1.00 28.74 C ATOM 1655 CG MET A 279 23.459 10.910 32.746 1.00 32.48 C ATOM 1656 SD MET A 279 24.341 9.409 32.243 1.00 41.72 S ATOM 1657 CE MET A 279 25.815 10.146 31.549 1.00 34.30 C ATOM 1658 N GLY A 280 20.036 11.097 35.800 1.00 30.04 N ATOM 1659 CA GLY A 280 18.799 10.731 36.465 1.00 29.03 C ATOM 1660 C GLY A 280 17.871 11.915 36.655 1.00 29.03 C ATOM 1661 O GLY A 280 16.664 11.819 36.433 1.00 28.08 O ATOM 1662 N VAL A 281 18.439 13.043 37.061 1.00 26.88 N ATOM 1663 CA VAL A 281 17.648 14.243 37.289 1.00 32.05 C ATOM 1664 C VAL A 281 17.091 14.778 35.970 1.00 36.24 C ATOM 1665 O VAL A 281 15.971 15.288 35.923 1.00 33.22 O ATOM 1666 CB VAL A 281 18.460 15.346 38.030 1.00 31.84 C ATOM 1667 CG1 VAL A 281 17.626 16.596 38.206 1.00 25.41 C ATOM 1668 CG2 VAL A 281 18.922 14.852 39.386 1.00 23.30 C ATOM 1669 N PHE A 282 17.870 14.660 34.895 1.00 34.19 N ATOM 1670 CA PHE A 282 17.397 15.077 33.577 1.00 23.76 C ATOM 1671 C PHE A 282 16.176 14.260 33.171 1.00 23.79 C ATOM 1672 O PHE A 282 15.193 14.808 32.715 1.00 24.64 O ATOM 1673 CB PHE A 282 18.504 14.942 32.536 1.00 23.90 C ATOM 1674 CG PHE A 282 18.055 15.227 31.130 1.00 28.01 C ATOM 1675 CD1 PHE A 282 18.209 16.505 30.581 1.00 22.81 C ATOM 1676 CD2 PHE A 282 17.478 14.223 30.350 1.00 15.85 C ATOM 1677 CE1 PHE A 282 17.801 16.781 29.277 1.00 17.51 C ATOM 1678 CE2 PHE A 282 17.059 14.491 29.056 1.00 19.68 C ATOM 1679 CZ PHE A 282 17.224 15.775 28.514 1.00 18.96 C ATOM 1680 N THR A 283 16.254 12.947 33.348 1.00 24.28 N ATOM 1681 CA THR A 283 15.135 12.058 33.086 1.00 24.17 C ATOM 1682 C THR A 283 13.919 12.426 33.934 1.00 28.85 C ATOM 1683 O THR A 283 12.833 12.634 33.412 1.00 36.45 O ATOM 1684 CB THR A 283 15.518 10.581 33.338 1.00 28.30 C ATOM 1685 OG1 THR A 283 16.713 10.265 32.608 1.00 27.27 O ATOM 1686 CG2 THR A 283 14.391 9.628 32.907 1.00 29.15 C ATOM 1687 N LEU A 284 14.094 12.506 35.243 1.00 30.79 N ATOM 1688 CA LEU A 284 12.993 12.908 36.110 1.00 38.11 C ATOM 1689 C LEU A 284 12.342 14.240 35.698 1.00 36.34 C ATOM 1690 O LEU A 284 11.169 14.462 35.972 1.00 38.76 O ATOM 1691 CB LEU A 284 13.450 12.980 37.570 1.00 39.24 C ATOM 1692 CG LEU A 284 13.911 11.659 38.174 1.00 49.58 C ATOM 1693 CD1 LEU A 284 14.251 11.856 39.636 1.00 46.06 C ATOM 1694 CD2 LEU A 284 12.854 10.569 37.998 1.00 40.05 C ATOM 1695 N CYS A 285 13.089 15.122 35.042 1.00 22.72 N ATOM 1696 CA CYS A 285 12.576 16.460 34.774 1.00 23.63 C ATOM 1697 C CYS A 285 11.844 16.601 33.450 1.00 31.72 C ATOM 1698 O CYS A 285 11.064 17.538 33.283 1.00 33.54 O ATOM 1699 CB CYS A 285 13.705 17.484 34.800 1.00 33.20 C ATOM 1700 SG CYS A 285 14.119 18.141 36.417 1.00 38.70 S ATOM 1701 N TRP A 286 12.108 15.689 32.511 1.00 30.43 N ATOM 1702 CA TRP A 286 11.595 15.805 31.146 1.00 20.54 C ATOM 1703 C TRP A 286 10.657 14.676 30.769 1.00 25.41 C ATOM 1704 O TRP A 286 9.769 14.851 29.946 1.00 28.19 O ATOM 1705 CB TRP A 286 12.744 15.867 30.145 1.00 19.64 C ATOM 1706 CG TRP A 286 13.288 17.235 29.972 1.00 19.89 C ATOM 1707 CD1 TRP A 286 14.525 17.667 30.321 1.00 17.16 C ATOM 1708 CD2 TRP A 286 12.604 18.371 29.428 1.00 19.43 C ATOM 1709 NE1 TRP A 286 14.662 19.000 30.017 1.00 17.58 N ATOM 1710 CE2 TRP A 286 13.499 19.456 29.464 1.00 15.44 C ATOM 1711 CE3 TRP A 286 11.325 18.574 28.909 1.00 19.34 C ATOM 1712 CZ2 TRP A 286 13.159 20.727 28.999 1.00 13.71 C ATOM 1713 CZ3 TRP A 286 10.989 19.835 28.443 1.00 18.63 C ATOM 1714 CH2 TRP A 286 11.903 20.894 28.494 1.00 17.00 C ATOM 1715 N LEU A 287 10.852 13.515 31.369 1.00 22.87 N ATOM 1716 CA LEU A 287 9.992 12.382 31.074 1.00 30.41 C ATOM 1717 C LEU A 287 8.499 12.708 31.280 1.00 29.75 C ATOM 1718 O LEU A 287 7.657 12.271 30.495 1.00 35.86 O ATOM 1719 CB LEU A 287 10.424 11.147 31.878 1.00 33.91 C ATOM 1720 CG LEU A 287 9.725 9.820 31.563 1.00 36.53 C ATOM 1721 CD1 LEU A 287 9.610 9.607 30.071 1.00 23.45 C ATOM 1722 CD2 LEU A 287 10.470 8.666 32.216 1.00 34.38 C ATOM 1723 N PRO A 288 8.162 13.482 32.321 1.00 29.36 N ATOM 1724 CA PRO A 288 6.731 13.798 32.460 1.00 28.86 C ATOM 1725 C PRO A 288 6.199 14.544 31.246 1.00 32.00 C ATOM 1726 O PRO A 288 5.182 14.143 30.673 1.00 36.36 O ATOM 1727 CB PRO A 288 6.676 14.703 33.700 1.00 29.48 C ATOM 1728 CG PRO A 288 7.923 14.353 34.489 1.00 33.48 C ATOM 1729 CD PRO A 288 8.966 13.967 33.461 1.00 33.01 C ATOM 1730 N PHE A 289 6.882 15.610 30.844 1.00 23.17 N ATOM 1731 CA PHE A 289 6.429 16.395 29.702 1.00 26.42 C ATOM 1732 C PHE A 289 6.283 15.598 28.384 1.00 34.74 C ATOM 1733 O PHE A 289 5.391 15.893 27.584 1.00 33.37 O ATOM 1734 CB PHE A 289 7.330 17.613 29.509 1.00 24.07 C ATOM 1735 CG PHE A 289 7.167 18.288 28.178 1.00 30.41 C ATOM 1736 CD1 PHE A 289 6.371 19.420 28.045 1.00 32.60 C ATOM 1737 CD2 PHE A 289 7.823 17.799 27.052 1.00 28.30 C ATOM 1738 CE1 PHE A 289 6.228 20.056 26.805 1.00 32.75 C ATOM 1739 CE2 PHE A 289 7.687 18.430 25.807 1.00 30.75 C ATOM 1740 CZ PHE A 289 6.893 19.561 25.685 1.00 28.80 C ATOM 1741 N PHE A 290 7.149 14.606 28.152 1.00 31.78 N ATOM 1742 CA PHE A 290 7.078 13.796 26.930 1.00 29.16 C ATOM 1743 C PHE A 290 6.060 12.684 27.063 1.00 34.27 C ATOM 1744 O PHE A 290 5.477 12.250 26.069 1.00 30.84 O ATOM 1745 CB PHE A 290 8.446 13.213 26.516 1.00 29.99 C ATOM 1746 CG PHE A 290 9.354 14.217 25.877 1.00 25.86 C ATOM 1747 CD1 PHE A 290 10.367 14.821 26.610 1.00 25.42 C ATOM 1748 CD2 PHE A 290 9.177 14.586 24.558 1.00 26.14 C ATOM 1749 CE1 PHE A 290 11.192 15.769 26.040 1.00 20.05 C ATOM 1750 CE2 PHE A 290 10.000 15.543 23.978 1.00 33.58 C ATOM 1751 CZ PHE A 290 11.005 16.138 24.726 1.00 26.98 C ATOM 1752 N LEU A 291 5.844 12.210 28.285 1.00 30.18 N ATOM 1753 CA LEU A 291 4.770 11.249 28.493 1.00 38.55 C ATOM 1754 C LEU A 291 3.410 11.910 28.260 1.00 37.01 C ATOM 1755 O LEU A 291 2.524 11.326 27.642 1.00 46.76 O ATOM 1756 CB LEU A 291 4.853 10.599 29.871 1.00 36.31 C ATOM 1757 CG LEU A 291 5.868 9.466 29.883 1.00 35.53 C ATOM 1758 CD1 LEU A 291 5.740 8.623 31.134 1.00 21.38 C ATOM 1759 CD2 LEU A 291 5.655 8.616 28.648 1.00 38.33 C ATOM 1760 N VAL A 292 3.258 13.141 28.728 1.00 30.20 N ATOM 1761 CA VAL A 292 2.011 13.868 28.532 1.00 34.07 C ATOM 1762 C VAL A 292 1.838 14.258 27.065 1.00 32.13 C ATOM 1763 O VAL A 292 0.735 14.554 26.604 1.00 34.65 O ATOM 1764 CB VAL A 292 1.931 15.087 29.492 1.00 30.82 C ATOM 1765 CG1 VAL A 292 1.535 16.353 28.771 1.00 29.45 C ATOM 1766 CG2 VAL A 292 0.987 14.776 30.627 1.00 29.79 C ATOM 1767 N ASN A 293 2.943 14.223 26.330 1.00 32.74 N ATOM 1768 CA ASN A 293 2.940 14.592 24.931 1.00 33.24 C ATOM 1769 C ASN A 293 2.428 13.456 24.060 1.00 34.83 C ATOM 1770 O ASN A 293 1.787 13.699 23.052 1.00 35.17 O ATOM 1771 CB ASN A 293 4.335 15.008 24.487 1.00 38.82 C ATOM 1772 CG ASN A 293 4.314 16.205 23.558 1.00 49.20 C ATOM 1773 OD1 ASN A 293 3.829 17.281 23.921 1.00 40.28 O ATOM 1774 ND2 ASN A 293 4.853 16.032 22.356 1.00 53.57 N ATOM 1775 N ILE A 294 2.711 12.216 24.452 1.00 41.48 N ATOM 1776 CA ILE A 294 2.213 11.051 23.727 1.00 36.70 C ATOM 1777 C ILE A 294 0.738 10.867 24.037 1.00 39.42 C ATOM 1778 O ILE A 294 −0.020 10.345 23.219 1.00 37.96 O ATOM 1779 CB ILE A 294 2.982 9.777 24.111 1.00 36.72 C ATOM 1780 CG1 ILE A 294 4.425 9.889 23.646 1.00 43.21 C ATOM 1781 CG2 ILE A 294 2.337 8.536 23.506 1.00 26.12 C ATOM 1782 CD1 ILE A 294 5.273 8.709 24.050 1.00 55.44 C ATOM 1783 N VAL A 295 0.331 11.316 25.219 1.00 29.39 N ATOM 1784 CA VAL A 295 −1.060 11.195 25.615 1.00 32.53 C ATOM 1785 C VAL A 295 −1.962 12.164 24.837 1.00 39.57 C ATOM 1786 O VAL A 295 −3.084 11.798 24.474 1.00 35.13 O ATOM 1787 CB VAL A 295 −1.238 11.336 27.145 1.00 38.23 C ATOM 1788 CG1 VAL A 295 −2.718 11.418 27.532 1.00 38.04 C ATOM 1789 CG2 VAL A 295 −0.570 10.172 27.846 1.00 30.65 C ATOM 1790 N ASN A 296 −1.491 13.383 24.562 1.00 32.31 N ATOM 1791 CA ASN A 296 −2.304 14.290 23.739 1.00 37.25 C ATOM 1792 C ASN A 296 −2.444 13.803 22.322 1.00 28.75 C ATOM 1793 O ASN A 296 −3.304 14.262 21.590 1.00 28.05 O ATOM 1794 CB ASN A 296 −1.795 15.732 23.745 1.00 34.25 C ATOM 1795 CG ASN A 296 −2.418 16.548 24.854 1.00 68.72 C ATOM 1796 OD1 ASN A 296 −3.610 16.867 24.823 1.00 68.31 O ATOM 1797 ND2 ASN A 296 −1.623 16.864 25.863 1.00 78.60 N ATOM 1798 N VAL A 297 −1.583 12.871 21.941 1.00 31.44 N ATOM 1799 CA VAL A 297 −1.654 12.283 20.623 1.00 40.37 C ATOM 1800 C VAL A 297 −2.849 11.335 20.552 1.00 38.56 C ATOM 1801 O VAL A 297 −3.630 11.386 19.602 1.00 43.26 O ATOM 1802 CB VAL A 297 −0.333 11.575 20.249 1.00 41.77 C ATOM 1803 CG1 VAL A 297 −0.565 10.541 19.145 1.00 35.23 C ATOM 1804 CG2 VAL A 297 0.716 12.607 19.835 1.00 27.83 C ATOM 1805 N PHE A 298 −3.002 10.510 21.583 1.00 30.68 N ATOM 1806 CA PHE A 298 −4.074 9.515 21.643 1.00 40.10 C ATOM 1807 C PHE A 298 −5.433 10.186 21.752 1.00 42.88 C ATOM 1808 O PHE A 298 −6.401 9.793 21.098 1.00 50.76 O ATOM 1809 CB PHE A 29B −3.842 8.563 22.820 1.00 40.28 C ATOM 1810 CG PHE A 298 −5.042 7.732 23.196 1.00 51.29 C ATOM 1811 CD1 PHE A 298 −5.526 6.750 22.347 1.00 52.77 C ATOM 1812 CD2 PHE A 298 −5.667 7.914 24.427 1.00 59.63 C ATOM 1813 CE1 PHE A 298 −6.629 5.983 22.709 1.00 59.59 C ATOM 1814 CE2 PHE A 298 −6.764 7.145 24.796 1.00 52.99 C ATOM 1815 CZ PHE A 298 −7.245 6.178 23.935 1.00 52.85 C ATOM 1816 N ASN A 299 −5.485 11.211 22.584 1.00 38.17 N ATOM 1817 CA ASN A 299 −6.692 11.963 22.821 1.00 33.80 C ATOM 1818 C ASN A 299 −6.252 13.335 23.290 1.00 33.16 C ATOM 1819 O ASN A 299 −5.761 13.488 24.397 1.00 36.04 O ATOM 1820 CB ASN A 299 −7.538 11.264 23.902 1.00 55.31 C ATOM 1821 CG ASN A 299 −8.950 11.869 24.074 1.00 56.13 C ATOM 1822 OD1 ASN A 299 −9.425 12.659 23.263 1.00 39.23 O ATOM 1823 ND2 ASN A 299 −9.620 11.472 25.146 1.00 64.78 N ATOM 1824 N ARG A 300 −6.391 14.335 22.433 1.00 41.37 N ATOM 1825 CA ARG A 300 −6.342 15.705 22.908 1.00 39.87 C ATOM 1826 C ARG A 300 −7.506 15.755 23.886 1.00 43.96 C ATOM 1827 O ARG A 300 −8.306 14.820 23.929 1.00 60.58 O ATOM 1828 CB ARG A 300 −6.509 16.675 21.734 1.00 46.81 C ATOM 1829 CG ARG A 300 −5.748 16.222 20.475 1.00 57.36 C ATOM 1830 CD ARG A 300 −5.202 17.383 19.637 1.00 78.04 C ATOM 1831 NE ARG A 300 −4.256 16.936 18.610 1.00 67.84 N ATOM 1832 CZ ARG A 300 −3.939 17.639 17.522 1.00 84.20 C ATOM 1833 NH1 ARG A 300 −4.495 18.827 17.305 1.00 78.04 N ATOM 1834 NH2 ARG A 300 −3.071 17.151 16.641 1.00 63.79 N ATOM 1835 N ASP A 301 −7.608 16.799 24.693 1.00 38.01 N ATOM 1836 CA ASP A 301 −8.663 16.860 25.728 1.00 48.40 C ATOM 1837 C ASP A 301 −8.390 15.974 26.963 1.00 42.36 C ATOM 1838 O ASP A 301 −8.778 16.323 28.073 1.00 55.68 O ATOM 1839 CB ASP A 301 −10.068 16.554 25.153 1.00 45.05 C ATOM 1840 CG ASP A 301 −10.513 17.563 24.077 1.00 58.21 C ATOM 1841 OD1 ASP A 301 −10.221 18.770 24.223 1.00 51.40 O ATOM 1842 OD2 ASP A 301 −11.165 17.151 23.083 1.00 51.99 O ATOM 1843 N LEU A 302 −7.708 14.847 26.778 1.00 48.76 N ATOM 1844 CA LEU A 302 −7.499 13.887 27.866 1.00 46.24 C ATOM 1845 C LEU A 302 −6.518 14.365 28.951 1.00 56.81 C ATOM 1846 O LEU A 302 −6.183 13.615 29.870 1.00 57.23 O ATOM 1847 CB LEU A 302 −7.038 12.539 27.297 1.00 47.16 C ATOM 1848 CG LEU A 302 −7.262 11.307 28.176 1.00 64.24 C ATOM 1849 CD1 LEU A 302 −8.674 10.780 28.013 1.00 73.09 C ATOM 1850 CD2 LEU A 302 −6.256 10.218 27.849 1.00 67.65 C ATOM 1851 N VAL A 303 −6.060 15.607 28.848 1.00 53.21 N ATOM 1852 CA VAL A 303 −5.088 16.146 29.797 1.00 47.03 C ATOM 1853 C VAL A 303 −4.986 17.662 29.673 1.00 48.63 C ATOM 1854 O VAL A 303 −4.795 18.194 28.578 1.00 52.65 O ATOM 1855 CB VAL A 303 −3.696 15.467 29.651 1.00 76.72 C ATOM 1856 CG1 VAL A 303 −2.597 16.489 29.339 1.00 52.44 C ATOM 1857 CG2 VAL A 303 −3.369 14.647 30.902 1.00 79.38 C ATOM 1858 N PRO A 304 −5.120 18.353 30.813 1.00 45.51 N ATOM 1859 CA PRO A 304 −5.423 19.784 30.968 1.00 42.15 C ATOM 1860 C PRO A 304 −4.234 20.698 30.753 1.00 50.04 C ATOM 1861 O PRO A 304 −3.168 20.480 31.337 1.00 52.26 O ATOM 1862 CB PRO A 304 −5.858 19.874 32.431 1.00 45.70 C ATOM 1863 CG PRO A 304 −5.055 18.788 33.089 1.00 45.19 C ATOM 1864 CD PRO A 304 −5.106 17.656 32.111 1.00 44.37 C ATOM 1865 N ASP A 305 −4.438 21.742 29.959 1.00 48.48 N ATOM 1866 CA ASP A 305 −3.359 22.652 29.578 1.00 50.77 C ATOM 1867 C ASP A 305 −2.421 23.018 30.738 1.00 53.64 C ATOM 1868 O ASP A 305 −1.201 23.065 30.566 1.00 53.35 O ATOM 1869 CB ASP A 305 −3.936 23.903 28.903 1.00 46.66 C ATOM 1870 CG ASP A 305 −4.797 23.565 27.676 1.00 80.33 C ATOM 1871 OD1 ASP A 305 −4.293 22.895 26.747 1.00 82.34 O ATOM 1872 OD2 ASP A 305 −5.981 23.966 27.638 1.00 76.24 O ATOM 1873 N TRP A 306 −2.982 23.258 31.919 1.00 55.32 N ATOM 1874 CA TRP A 306 −2.169 23.657 33.070 1.00 48.34 C ATOM 1875 C TRP A 306 −1.138 22.583 33.438 1.00 44.19 C ATOM 1876 O TRP A 306 −0.040 22.902 33.897 1.00 37.44 O ATOM 1877 CB TRP A 306 −3.049 24.007 34.291 1.00 38.86 C ATOM 1878 CG TRP A 306 −3.675 22.809 34.925 1.00 41.79 C ATOM 1879 CD1 TRP A 306 −4.932 22.330 34.700 1.00 42.75 C ATOM 1880 CD2 TRP A 306 −3.062 21.909 35.862 1.00 39.45 C ATOM 1881 NE1 TRP A 306 −5.142 21.192 35.446 1.00 44.90 N ATOM 1882 CE2 TRP A 306 −4.009 20.912 36.164 1.00 36.69 C ATOM 1883 CE3 TRP A 306 −1.799 21.843 36.464 1.00 50.61 C ATOM 1884 CZ2 TRP A 306 −3.741 19.867 37.050 1.00 39.13 C ATOM 1885 CZ3 TRP A 306 −1.533 20.803 37.349 1.00 47.84 C ATOM 1886 CH2 TRP A 306 −2.502 19.832 37.633 1.00 35.00 C ATOM 1887 N LEU A 307 −1.495 21.314 33.253 1.00 40.36 N ATOM 1888 CA LEU A 307 −0.572 20.234 33.565 1.00 43.17 C ATOM 1889 C LEU A 307 0.559 20.220 32.532 1.00 42.75 C ATOM 1890 O LEU A 307 1.667 19.736 32.780 1.00 34.32 O ATOM 1891 CB LEU A 307 −1.288 18.884 33.605 1.00 34.20 C ATOM 1892 CG LEU A 307 −0.356 17.700 33.904 1.00 38.15 C ATOM 1893 CD1 LEU A 307 0.496 17.953 35.149 1.00 37.24 C ATOM 1894 CD2 LEU A 307 −1.131 16.409 34.051 1.00 44.32 C ATOM 1895 N PHE A 308 0.272 20.774 31.368 1.00 40.30 N ATOM 1896 CA PHE A 308 1.271 20.847 30.330 1.00 39.85 C ATOM 1897 C PHE A 308 2.261 21.924 30.695 1.00 39.32 C ATOM 1898 O PHE A 308 3.469 21.742 30.573 1.00 40.33 O ATOM 1899 CB PHE A 308 0.622 21.177 28.993 1.00 40.57 C ATOM 1900 CG PHE A 308 0.907 20.170 27.941 1.00 45.51 C ATOM 1901 CD1 PHE A 308 −0.118 19.478 27.328 1.00 46.52 C ATOM 1902 CD2 PHE A 308 2.213 19.882 27.588 1.00 56.88 C ATOM 1903 CE1 PHE A 308 0.154 18.539 26.365 1.00 43.73 C ATOM 1904 CE2 PHE A 308 2.491 18.935 26.623 1.00 53.41 C ATOM 1905 CZ PHE A 308 1.458 18.261 26.014 1.00 47.50 C ATOM 1906 N VAL A 309 1.743 23.056 31.149 1.00 34.05 N ATOM 1907 CA VAL A 309 2.607 24.162 31.490 1.00 31.94 C ATOM 1908 C VAL A 309 3.512 23.742 32.636 1.00 36.51 C ATOM 1909 O VAL A 309 4.712 24.028 32.632 1.00 38.80 O ATOM 1910 CB VAL A 309 1.811 25.429 31.865 1.00 36.58 C ATOM 1911 CG1 VAL A 309 2.714 26.435 32.538 1.00 31.61 C ATOM 1912 CG2 VAL A 309 1.188 26.050 30.627 1.00 31.16 C ATOM 1913 N ALA A 310 2.944 23.044 33.609 1.00 27.43 N ATOM 1914 CA ALA A 310 3.721 22.657 34.777 1.00 31.61 C ATOM 1915 C ALA A 310 4.849 21.710 34.411 1.00 29.82 C ATOM 1916 O ALA A 310 5.999 21.954 34.753 1.00 28.17 O ATOM 1917 CB ALA A 310 2.833 22.035 35.837 1.00 33.03 C ATOM 1918 N PHE A 311 4.514 20.619 33.731 1.00 30.28 N ATOM 1919 CA PHE A 311 5.521 19.662 33.289 1.00 29.01 C ATOM 1920 C PHE A 311 6.588 20.283 32.390 1.00 24.16 C ATOM 1921 O PHE A 311 7.755 19.901 32.462 1.00 19.79 O ATOM 1922 CB PHE A 311 4.872 18.462 32.602 1.00 28.06 C ATOM 1923 CG PHE A 311 4.267 17.489 33.557 1.00 30.77 C ATOM 1924 CD1 PHE A 311 3.303 16.591 33.143 1.00 37.91 C ATOM 1925 CD2 PHE A 311 4.647 17.488 34.883 1.00 31.39 C ATOM 1926 CE1 PHE A 311 2.745 15.691 34.030 1.00 38.99 C ATOM 1927 CE2 PHE A 311 4.092 16.594 35.777 1.00 32.21 C ATOM 1928 CZ PHE A 311 3.142 15.694 35.351 1.00 27.81 C ATOM 1929 N ASN A 312 6.193 21.243 31.559 1.00 22.04 N ATOM 1930 CA ASN A 312 7.153 21.945 30.719 1.00 30.68 C ATOM 1931 C ASN A 312 8.137 22.802 31.520 1.00 27.18 C ATOM 1932 O ASN A 312 9.302 22.942 31.142 1.00 27.28 O ATOM 1933 CB ASN A 312 6.448 22.796 29.658 1.00 27.40 C ATOM 1934 CG ASN A 312 7.297 22.990 28.399 1.00 24.90 C ATOM 1935 OD1 ASN A 312 6.808 23.455 27.375 1.00 26.88 O ATOM 1936 ND2 ASN A 312 8.570 22.630 28.478 1.00 30.58 N ATOM 1937 N TRP A 313 7.671 23.373 32.621 1.00 26.32 N ATOM 1938 CA TRP A 313 8.535 24.187 33.461 1.00 23.34 C ATOM 1939 C TRP A 313 9.364 23.320 34.364 1.00 21.46 C ATOM 1940 O TRP A 313 10.449 23.723 34.785 1.00 27.58 O ATOM 1941 CB TRP A 313 7.736 25.225 34.256 1.00 29.94 C ATOM 1942 CG TRP A 313 7.329 26.352 33.370 1.00 37.79 C ATOM 1943 CD1 TRP A 313 6.225 26.401 32.559 1.00 34.07 C ATOM 1944 CD2 TRP A 313 8.041 27.576 33.154 1.00 37.87 C ATOM 1945 NE1 TRP A 313 6.200 27.588 31.866 1.00 38.51 N ATOM 1946 CE2 TRP A 313 7.303 28.329 32.208 1.00 40.02 C ATOM 1947 CE3 TRP A 313 9.224 28.116 33.673 1.00 36.00 C ATOM 1948 CZ2 TRP A 313 7.710 29.594 31.769 1.00 32.64 C ATOM 1949 CZ3 TRP A 313 9.626 29.370 33.237 1.00 45.28 C ATOM 1950 CH2 TRP A 313 8.867 30.096 32.290 1.00 35.80 C ATOM 1951 N LEU A 314 8.870 22.123 34.655 1.00 14.43 N ATOM 1952 CA LEU A 314 9.663 21.177 35.419 1.00 18.61 C ATOM 1953 C LEU A 314 10.956 20.893 34.648 1.00 30.32 C ATOM 1954 O LEU A 314 12.055 20.939 35.208 1.00 30.52 O ATOM 1955 CB LEU A 314 8.892 19.892 35.658 1.00 21.05 C ATOM 1956 CG LEU A 314 9.790 18.803 36.234 1.00 28.28 C ATOM 1957 CD1 LEU A 314 10.455 19.297 37.511 1.00 18.78 C ATOM 1958 CD2 LEU A 314 9.007 17.520 36.466 1.00 26.58 C ATOM 1959 N GLY A 315 10.812 20.616 33.357 1.00 22.34 N ATOM 1960 CA GLY A 315 11.943 20.462 32.465 1.00 22.45 C ATOM 1961 C GLY A 315 12.849 21.678 32.305 1.00 24.40 C ATOM 1962 O GLY A 315 14.074 21.533 32.208 1.00 21.05 O ATOM 1963 N TYR A 316 12.278 22.881 32.249 1.00 21.26 N ATOM 1964 CA TYR A 316 13.127 24.055 32.185 1.00 20.00 C ATOM 1965 C TYR A 316 13.940 24.146 33.464 1.00 25.77 C ATOM 1966 O TYR A 316 15.116 24.483 33.432 1.00 31.20 O ATOM 1967 CB TYR A 316 12.337 25.348 32.029 1.00 26.18 C ATOM 1968 CG TYR A 316 11.676 25.589 30.690 1.00 30.32 C ATOM 1969 CD1 TYR A 316 10.502 26.340 30.623 1.00 25.91 C ATOM 1970 CD2 TYR A 316 12.214 25.085 29.495 1.00 24.72 C ATOM 1971 CE1 TYR A 316 9.876 26.579 29.425 1.00 32.87 C ATOM 1972 CE2 TYR A 316 11.583 25.322 28.268 1.00 25.69 C ATOM 1973 CZ TYR A 316 10.405 26.069 28.251 1.00 35.54 C ATOM 1974 OH TYR A 316 9.727 26.336 27.087 1.00 23.78 O ATOM 1975 N ALA A 317 13.316 23.858 34.601 1.00 27.10 N ATOM 1976 CA ALA A 317 14.009 24.011 35.880 1.00 31.56 C ATOM 1977 C ALA A 317 15.267 23.141 35.925 1.00 30.12 C ATOM 1978 O ALA A 317 16.224 23.449 36.633 1.00 36.10 O ATOM 1979 CB ALA A 317 13.077 23.717 37.062 1.00 25.70 C ATOM 1980 N ASN A 318 15.263 22.066 35.148 1.00 25.92 N ATOM 1981 CA ASN A 318 16.436 21.222 34.997 1.00 28.36 C ATOM 1982 C ASN A 318 17.718 21.986 34.639 1.00 31.01 C ATOM 1983 O ASN A 318 18.802 21.587 35.051 1.00 38.96 O ATOM 1984 CB ASN A 318 16.175 20.133 33.958 1.00 29.44 C ATOM 1985 CG ASN A 318 17.347 19.183 33.804 1.00 29.62 C ATOM 1986 OD1 ASN A 318 17.396 18.146 34.458 1.00 34.97 O ATOM 1987 ND2 ASN A 318 18.297 19.532 32.933 1.00 29.17 N ATOM 1988 N SER A 319 17.604 23.069 33.873 1.00 25.40 N ATOM 1989 CA SER A 319 18.776 23.863 33.496 1.00 29.82 C ATOM 1990 C SER A 319 19.453 24.537 34.696 1.00 34.93 C ATOM 1991 O SER A 319 20.597 24.987 34.599 1.00 28.00 O ATOM 1992 CB SER A 319 18.411 24.938 32.469 1.00 26.81 C ATOM 1993 OG SER A 319 18.082 24.378 31.220 1.00 27.46 O ATOM 1994 N ALA A 320 18.738 24.610 35.818 1.00 34.25 N ATOM 1995 CA ALA A 320 19.261 25.240 37.027 1.00 33.94 C ATOM 1996 C ALA A 320 19.871 24.235 38.017 1.00 32.35 C ATOM 1997 O ALA A 320 20.658 24.609 38.876 1.00 33.27 O ATOM 1998 CB ALA A 320 18.182 26.075 37.695 1.00 28.56 C ATOM 1999 N MET A 321 19.527 22.961 37.869 1.00 29.51 N ATOM 2000 CA MET A 321 20.030 21.913 38.756 1.00 35.23 C ATOM 2001 C MET A 321 21.503 21.528 38.619 1.00 36.29 C ATOM 2002 O MET A 321 22.172 21.264 39.614 1.00 39.19 O ATOM 2003 CB MET A 321 19.184 20.657 38.603 1.00 36.04 C ATOM 2004 CG MET A 321 17.824 20.789 39.226 1.00 43.97 C ATOM 2005 SD MET A 321 16.684 19.595 38.548 1.00 52.50 S ATOM 2006 CE MET A 321 15.171 20.088 39.381 1.00 40.72 C ATOM 2007 N ASN A 322 22.009 21.458 37.397 1.00 38.22 N ATOM 2008 CA ASN A 322 23.354 20.924 37.197 1.00 38.64 C ATOM 2009 C ASN A 322 24.455 21.584 38.041 1.00 40.39 C ATOM 2010 O ASN A 322 25.216 20.886 38.708 1.00 41.43 O ATOM 2011 CB ASN A 322 23.731 20.893 35.710 1.00 49.34 C ATOM 2012 CG ASN A 322 23.128 19.706 34.980 1.00 40.88 C ATOM 2013 OD1 ASN A 322 21.940 19.427 35.102 1.00 46.73 O ATOM 2014 ND2 ASN A 322 23.947 19.006 34.213 1.00 36.87 N ATOM 2015 N PRO A 323 24.543 22.926 38.020 1.00 39.71 N ATOM 2016 CA PRO A 323 25.602 23.590 38.791 1.00 42.67 C ATOM 2017 C PRO A 323 25.528 23.231 40.280 1.00 41.51 C ATOM 2018 O PRO A 323 26.538 22.909 40.903 1.00 42.81 O ATOM 2019 CB PRO A 323 25.317 25.083 38.574 1.00 40.26 C ATOM 2020 CG PRO A 323 24.495 25.148 37.332 1.00 43.40 C ATOM 2021 CD PRO A 323 23.677 23.891 37.322 1.00 43.03 C ATOM 2022 N ILE A 324 24.329 23.277 40.838 1.00 29.28 N ATOM 2023 CA ILE A 324 24.123 22.792 42.187 1.00 37.13 C ATOM 2024 C ILE A 324 24.746 21.402 42.366 1.00 35.21 C ATOM 2025 O ILE A 324 25.602 21.209 43.216 1.00 44.57 O ATOM 2026 CB ILE A 324 22.618 22.785 42.557 1.00 37.02 C ATOM 2027 CG1 ILE A 324 22.136 24.215 42.828 1.00 27.30 C ATOM 2028 CG2 ILE A 324 22.356 21.879 43.759 1.00 28.99 C ATOM 2029 CD1 ILE A 324 20.626 24.373 42.836 1.00 38.99 C ATOM 2030 N ILE A 325 24.327 20.437 41.560 1.00 36.21 N ATOM 2031 CA ILE A 325 24.866 19.079 41.660 1.00 47.07 C ATOM 2032 C ILE A 325 26.412 18.992 41.622 1.00 46.54 C ATOM 2033 O ILE A 325 27.001 18.111 42.249 1.00 31.80 O ATOM 2034 CB ILE A 325 24.250 18.172 40.567 1.00 39.87 C ATOM 2035 CG1 ILE A 325 22.734 18.132 40.722 1.00 31.25 C ATOM 2036 CG2 ILE A 325 24.842 16.758 40.609 1.00 39.38 C ATOM 2037 CD1 ILE A 325 22.011 17.461 39.557 1.00 30.29 C ATOM 2038 N TYR A 326 27.059 19.893 40.880 1.00 38.35 N ATOM 2039 CA TYR A 326 28.513 19.866 40.748 1.00 42.65 C ATOM 2040 C TYR A 326 29.206 20.323 42.021 1.00 54.64 C ATOM 2041 O TYR A 326 30.425 20.207 42.152 1.00 53.74 O ATOM 2042 CB TYR A 326 28.991 20.775 39.619 1.00 50.34 C ATOM 2043 CG TYR A 326 28.528 20.386 38.247 1.00 47.66 C ATOM 2044 CD1 TYR A 326 28.263 21.358 37.290 1.00 46.78 C ATOM 2045 CD2 TYR A 326 28.347 19.057 37.904 1.00 49.11 C ATOM 2046 CE1 TYR A 326 27.836 21.021 36.032 1.00 38.16 C ATOM 2047 CE2 TYR A 326 27.914 18.705 36.641 1.00 45.70 C ATOM 2048 CZ TYR A 326 27.660 19.693 35.714 1.00 42.81 C ATOM 2049 OH TYR A 326 27.226 19.356 34.459 1.00 47.78 O ATOM 2050 N CYS A 327 28.437 20.876 42.947 1.00 47.21 N ATOM 2051 CA CYS A 327 29.007 21.312 44.205 1.00 40.99 C ATOM 2052 C CYS A 327 29.341 20.101 45.068 1.00 49.85 C ATOM 2053 O CYS A 327 30.042 20.216 46.071 1.00 57.22 O ATOM 2054 CB CYS A 327 28.072 22.285 44.905 1.00 34.61 C ATOM 2055 SG CYS A 327 27.994 23.895 44.076 1.00 56.73 S ATOM 2056 N ARG A 328 28.859 18.936 44.641 1.00 46.95 N ATOM 2057 CA ARG A 328 29.226 17.658 45.243 1.00 45.77 C ATOM 2058 C ARG A 328 30.715 17.397 45.115 1.00 55.68 C ATOM 2059 O ARG A 328 31.317 16.768 45.977 1.00 61.95 O ATOM 2060 CB ARG A 328 28.486 16.521 44.558 1.00 43.92 C ATOM 2061 CG ARG A 328 27.017 16.417 44.895 1.00 56.15 C ATOM 2062 CD ARG A 328 26.452 15.285 44.095 1.00 47.45 C ATOM 2063 NE ARG A 328 27.521 14.340 43.808 1.00 56.68 N ATOM 2064 CZ ARG A 328 27.670 13.169 44.417 1.00 66.08 C ATOM 2065 NH1 ARG A 328 26.794 12.784 45.337 1.00 65.47 N ATOM 2066 NH2 ARG A 328 28.686 12.375 44.095 1.00 59.85 N ATOM 2067 N SER A 329 31.301 17.855 44.016 1.00 64.43 N ATOM 2068 CA SER A 329 32.741 17.761 43.826 1.00 62.35 C ATOM 2069 C SER A 329 33.434 18.853 44.615 1.00 69.01 C ATOM 2070 O SER A 329 32.899 19.949 44.768 1.00 66.26 O ATOM 2071 CB SER A 329 33.108 17.906 42.353 1.00 69.85 C ATOM 2072 OG SER A 329 34.434 18.390 42.217 1.00 67.34 O ATOM 2073 N PRO A 330 34.640 18.557 45.114 1.00 84.00 N ATOM 2074 CA PRO A 330 35.419 19.505 45.915 1.00 77.72 C ATOM 2075 C PRO A 330 36.052 20.573 45.031 1.00 75.12 C ATOM 2076 O PRO A 330 36.226 21.709 45.472 1.00 66.99 O ATOM 2077 CB PRO A 330 36.509 18.625 46.544 1.00 81.03 C ATOM 2078 CG PRO A 330 36.117 17.188 46.226 1.00 93.05 C ATOM 2079 CD PRO A 330 35.329 17.266 44.968 1.00 88.46 C ATOM 2080 N ASP A 331 36.381 20.201 43.795 1.00 77.68 N ATOM 2081 CA ASP A 331 37.051 21.098 42.857 1.00 75.36 C ATOM 2082 C ASP A 331 36.157 22.247 42.402 1.00 70.53 C ATOM 2083 O ASP A 331 36.564 23.409 42.445 1.00 65.25 O ATOM 2084 CB ASP A 331 37.537 20.321 41.634 1.00 88.89 C ATOM 2085 CG ASP A 331 38.343 19.098 42.005 1.00 102.44 C ATOM 2086 OD1 ASP A 331 38.749 18.992 43.183 1.00 99.44 O ATOM 2087 OD2 ASP A 331 38.570 18.244 41.120 1.00 112.25 O ATOM 2088 N PHE A 332 34.950 21.916 41.947 1.00 71.27 N ATOM 2089 CA PHE A 332 33.987 22.929 41.523 1.00 69.05 C ATOM 2090 C PHE A 332 33.677 23.857 42.689 1.00 71.72 C ATOM 2091 O PHE A 332 33.635 25.079 42.534 1.00 64.41 O ATOM 2092 CB PHE A 332 32.691 22.280 41.027 1.00 63.76 C ATOM 2093 CG PHE A 332 32.760 21.774 39.609 1.00 66.85 C ATOM 2094 CD1 PHE A 332 32.999 20.429 39.345 1.00 59.21 C ATOM 2095 CD2 PHE A 332 32.567 22.642 38.536 1.00 66.38 C ATOM 2096 CE1 PHE A 332 33.053 19.953 38.036 1.00 59.19 C ATOM 2097 CE2 PHE A 332 32.626 22.175 37.223 1.00 60.53 C ATOM 2098 CZ PHE A 332 32.868 20.824 36.974 1.00 52.06 C ATOM 2099 N ARG A 333 33.464 23.252 43.855 1.00 71.60 N ATOM 2100 CA ARG A 333 33.176 23.966 45.094 1.00 58.60 C ATOM 2101 C ARG A 333 34.287 24.972 45.401 1.00 62.91 C ATOM 2102 O ARG A 333 34.026 26.170 45.519 1.00 60.30 O ATOM 2103 CB ARG A 333 33.053 22.952 46.228 1.00 66.66 C ATOM 2104 CG ARG A 333 31.920 23.191 47.198 1.00 68.59 C ATOM 2105 CD ARG A 333 31.584 21.890 47.920 1.00 76.56 C ATOM 2106 NE ARG A 333 32.742 20.997 48.017 1.00 84.78 N ATOM 2107 CZ ARG A 333 32.696 19.751 48.486 1.00 84.02 C ATOM 2108 NH1 ARG A 333 31.547 19.244 48.910 1.00 78.43 N ATOM 2109 NH2 ARG A 333 33.800 19.011 48.534 1.00 68.20 N ATOM 2110 N LYS A 334 35.521 24.475 45.527 1.00 65.19 N ATOM 2111 CA LYS A 334 36.696 25.327 45.717 1.00 68.09 C ATOM 2112 C LYS A 334 36.688 26.471 44.710 1.00 70.85 C ATOM 2113 O LYS A 334 36.854 27.642 45.069 1.00 62.94 O ATOM 2114 CB LYS A 334 37.995 24.530 45.522 1.00 81.57 C ATOM 2115 CG LYS A 334 38.332 23.473 46.576 1.00 83.57 C ATOM 2116 CD LYS A 334 39.713 22.865 46.278 1.00 91.78 C ATOM 2117 CE LYS A 334 39.839 21.418 46.761 1.00 93.06 C ATOM 2118 NZ LYS A 334 40.917 20.659 46.041 1.00 61.77 N ATOM 2119 N ALA A 335 36.499 26.107 43.443 1.00 69.41 N ATOM 2120 CA ALA A 335 36.560 27.047 42.330 1.00 68.42 C ATOM 2121 C ALA A 335 35.402 28.037 42.307 1.00 67.02 C ATOM 2122 O ALA A 335 35.588 29.200 41.946 1.00 63.39 O ATOM 2123 CB ALA A 335 36.638 26.297 41.014 1.00 69.49 C ATOM 2124 N PHE A 336 34.209 27.576 42.672 1.00 68.84 N ATOM 2125 CA PHE A 336 33.059 28.466 42.783 1.00 73.90 C ATOM 2126 C PHE A 336 33.341 29.534 43.843 1.00 75.96 C ATOM 2127 O PHE A 336 32.929 30.688 43.706 1.00 79.23 O ATOM 2128 CB PHE A 336 31.784 27.698 43.160 1.00 74.10 C ATOM 2129 CG PHE A 336 31.292 26.739 42.101 1.00 77.12 C ATOM 2130 CD1 PHE A 336 31.368 27.058 40.754 1.00 71.25 C ATOM 2131 CD2 PHE A 336 30.711 25.529 42.466 1.00 73.70 C ATOM 2132 CE1 PHE A 336 30.903 26.175 39.788 1.00 64.33 C ATOM 2133 CE2 PHE A 336 30.247 24.643 41.508 1.00 69.53 C ATOM 2134 CZ PHE A 336 30.346 24.967 40.165 1.00 65.33 C ATOM 2135 N LYS A 337 34.046 29.143 44.899 1.00 77.88 N ATOM 2136 CA LYS A 337 34.337 30.055 46.005 1.00 82.32 C ATOM 2137 C LYS A 337 35.461 31.046 45.671 1.00 81.10 C ATOM 2138 O LYS A 337 35.337 32.240 45.948 1.00 77.24 O ATOM 2139 CB LYS A 337 34.636 29.274 47.291 1.00 78.45 C ATOM 2140 CG LYS A 337 33.492 28.361 47.726 1.00 82.00 C ATOM 2141 CD LYS A 337 33.592 27.961 49.196 1.00 89.92 C ATOM 2142 CE LYS A 337 32.410 27.086 49.612 1.00 89.55 C ATOM 2143 NZ LYS A 337 32.424 26.743 51.064 1.00 84.38 N ATOM 2144 N ARG A 338 36.552 30.556 45.085 1.00 71.18 N ATOM 2145 CA ARG A 338 37.571 31.454 44.553 1.00 83.11 C ATOM 2146 C ARG A 338 36.870 32.534 43.735 1.00 86.54 C ATOM 2147 O ARG A 338 37.009 33.729 44.001 1.00 85.59 O ATOM 2148 CB ARG A 338 38.542 30.711 43.632 1.00 86.26 C ATOM 2149 CG ARG A 338 39.331 29.577 44.257 1.00 95.44 C ATOM 2150 CD ARG A 338 40.254 28.965 43.205 1.00 106.82 C ATOM 2151 NE ARG A 338 41.311 28.142 43.788 1.00 135.48 N ATOM 2152 CZ ARG A 338 42.394 27.734 43.130 1.00 134.67 C ATOM 2153 NH1 ARG A 338 42.575 28.073 41.858 1.00 122.13 N ATOM 2154 NH2 ARG A 338 43.303 26.988 43.747 1.00 114.82 N ATOM 2155 N LEU A 339 36.106 32.087 42.741 1.00 88.89 N ATOM 2156 CA LEU A 339 35.394 32.963 41.811 1.00 84.99 C ATOM 2157 C LEU A 339 34.468 33.969 42.491 1.00 88.07 C ATOM 2158 O LEU A 339 34.228 35.055 41.963 1.00 85.96 O ATOM 2159 CB LEU A 339 34.568 32.126 40.832 1.00 80.83 C ATOM 2160 CG LEU A 339 35.278 31.243 39.805 1.00 90.75 C ATOM 2161 CD1 LEU A 339 34.295 30.218 39.251 1.00 81.20 C ATOM 2162 CD2 LEU A 339 35.892 32.074 38.677 1.00 76.22 C ATOM 2163 N LEU A 340 33.930 33.602 43.648 1.00 86.03 N ATOM 2164 CA LEU A 340 33.013 34.489 44.359 1.00 90.06 C ATOM 2165 C LEU A 340 33.729 35.309 45.441 1.00 85.66 C ATOM 2166 O LEU A 340 33.189 35.536 46.524 1.00 77.85 O ATOM 2167 CB LEU A 340 31.837 33.692 44.933 1.00 85.58 C ATOM 2168 CG LEU A 340 30.902 33.092 43.877 1.00 78.39 C ATOM 2169 CD1 LEU A 340 30.206 31.825 44.372 1.00 80.26 C ATOM 2170 CD2 LEU A 340 29.885 34.129 43.412 1.00 72.07 C ATOM 2171 N ALA A 341 34.938 35.764 45.117 1.00 82.14 N ATOM 2172 CA ALA A 341 35.721 36.624 45.998 1.00 73.03 C ATOM 2173 C ALA A 341 35.692 36.132 47.444 1.00 106.96 C ATOM 2174 O ALA A 341 35.595 36.925 48.383 1.00 120.03 O ATOM 2175 CB ALA A 341 35.231 38.070 45.907 1.00 65.86 C ATOM 2176 C16 PDL A 400 6.169 18.015 19.883 1.00 46.49 C ATOM 2177 N3 PDL A 400 5.174 17.982 19.326 1.00 44.91 N ATOM 2178 N1 PDL A 400 8.722 17.389 19.902 1.00 38.18 N ATOM 2179 C1 PDL A 400 7.505 18.124 20.397 1.00 33.65 C ATOM 2180 C2 PDL A 400 7.917 18.971 21.577 1.00 29.80 C ATOM 2181 C3 PDL A 400 9.361 18.738 21.797 1.00 30.22 C ATOM 2182 C4 PDL A 400 10.316 19.291 22.834 1.00 36.02 C ATOM 2183 C5 PDL A 400 11.785 18.889 22.854 1.00 31.90 C ATOM 2184 C6 PDL A 400 12.291 17.900 21.805 1.00 36.57 C ATOM 2185 C7 PDL A 400 11.339 17.331 20.759 1.00 35.83 C ATOM 2186 C8 PDL A 400 9.867 17.756 20.761 1.00 34.90 C ATOM 2187 O1 PDL A 400 9.793 20.149 23.793 1.00 42.13 O ATOM 2188 C9 PDL A 400 10.417 21.358 24.062 1.00 27.23 C ATOM 2189 C10 PDL A 400 9.377 22.051 24.916 1.00 24.02 C ATOM 2190 O2 PDL A 400 10.052 22.568 26.032 1.00 26.04 O ATOM 2191 C11 PDL A 400 8.718 23.113 24.011 1.00 20.17 C ATOM 2192 N2 PDL A 400 8.102 24.220 24.731 1.00 25.80 N ATOM 2193 C12 PDL A 400 6.899 24.689 24.034 1.00 31.93 C ATOM 2194 C13 PDL A 400 5.911 23.506 23.823 1.00 20.39 C ATOM 2195 C14 PDL A 400 7.299 25.362 22.685 1.00 17.20 C ATOM 2196 C15 PDL A 400 6.254 25.714 24.991 1.00 16.73 C ATOM 2197 NA NA A 401 0.643 32.135 15.873 1.00 36.22 Na

TABLE B CRYST1 55.500 86.800 95.500 67.60 73.30 85.80 P1 SCALE1 0.018018 −0.001323 −0.005298 0.00000 SCALE2 0.000000 0.011552 −0.004700 0.00000 SCALE3 0.000000 0.000000 0.011803 0.00000 ATOM 2198 N GLN B 31 36.149 −5.203 −24.403 1.00 81.77 N ATOM 2199 CA GLN B 31 34.722 −5.513 −24.547 1.00 89.90 C ATOM 2200 C GLN B 31 34.186 −6.397 −23.410 1.00 84.77 C ATOM 2201 O GLN B 31 33.071 −6.915 −23.475 1.00 90.50 O ATOM 2202 CB GLN B 31 34.431 −6.163 −25.902 1.00 90.00 C ATOM 2203 CG GLN B 31 33.264 −5.532 −26.640 1.00 80.74 C ATOM 2204 CD GLN B 31 33.722 −4.445 −27.585 1.00 69.73 C ATOM 2205 OE1 GLN B 31 34.894 −4.072 −27.590 1.00 70.46 O ATOM 2206 NE2 GLN B 31 32.808 −3.948 −28.408 1.00 58.43 N ATOM 2207 N TRP B 32 35.014 −6.597 −22.395 1.00 82.72 N ATOM 2208 CA TRP B 32 34.565 −6.977 −21.065 1.00 65.66 C ATOM 2209 C TRP B 32 33.421 −6.044 −20.645 1.00 72.87 C ATOM 2210 O TRP B 32 32.620 −6.382 −19.776 1.00 77.95 O ATOM 2211 CB TRP B 32 35.753 −6.878 −20.107 1.00 59.16 C ATOM 2212 CG TRP B 32 35.424 −6.874 −18.657 1.00 81.99 C ATOM 2213 CD1 TRP B 32 35.362 −7.958 −17.828 1.00 90.78 C ATOM 2214 CD2 TRP B 32 35.149 −5.724 −17.841 1.00 83.95 C ATOM 2215 NE1 TRP B 32 35.049 −7.556 −16.549 1.00 100.38 N ATOM 2216 CE2 TRP B 32 34.912 −6.192 −16.529 1.00 96.28 C ATOM 2217 CE3 TRP B 32 35.066 −4.350 −18.094 1.00 67.70 C ATOM 2218 CZ2 TRP B 32 34.597 −5.328 −15.470 1.00 77.74 C ATOM 2219 CZ3 TRP B 32 34.754 −3.494 −17.042 1.00 64.94 C ATOM 2220 CH2 TRP B 32 34.524 −3.988 −15.748 1.00 65.52 C ATOM 2221 N GLU B 33 33.341 −4.877 −21.285 1.00 72.51 N ATOM 2222 CA GLU B 33 32.250 −3.927 −21.059 1.00 58.20 C ATOM 2223 C GLU B 33 30.899 −4.501 −21.460 1.00 57.23 C ATOM 2224 O GLU B 33 29.879 −4.144 −20.883 1.00 60.36 O ATOM 2225 CB GLU B 33 32.481 −2.625 −21.838 1.00 59.22 C ATOM 2226 CG GLU B 33 31.228 −1.736 −21.943 1.00 65.68 C ATOM 2227 CD GLU B 33 31.378 −0.539 −22.895 1.00 78.55 C ATOM 2228 OE1 GLU B 33 32.441 −0.400 −23.543 1.00 76.32 O ATOM 2229 OE2 GLU B 33 30.424 0.271 −22.993 1.00 60.84 O ATOM 2230 N ALA B 34 30.891 −5.378 −22.459 1.00 68.27 N ATOM 2231 CA ALA B 34 29.642 −5.896 −23.014 1.00 65.86 C ATOM 2232 C ALA B 34 29.013 −6.991 −22.155 1.00 67.93 C ATOM 2233 O ALA B 34 27.793 −7.026 −21.990 1.00 64.00 O ATOM 2234 CB ALA B 34 29.856 −6.389 −24.432 1.00 63.85 C ATOM 2235 N GLY B 35 29.842 −7.882 −21.616 1.00 62.49 N ATOM 2236 CA GLY B 35 29.356 −8.930 −20.738 1.00 48.88 C ATOM 2237 C GLY B 35 28.877 −8.348 −19.421 1.00 60.74 C ATOM 2238 O GLY B 35 27.940 −8.851 −18.798 1.00 62.64 O ATOM 2239 N MET B 36 29.528 −7.270 −19.001 1.00 59.62 N ATOM 2240 CA MET B 36 29.181 −6.589 −17.765 1.00 51.03 C ATOM 2241 C MET B 36 27.827 −5.883 −17.916 1.00 60.69 C ATOM 2242 O MET B 36 26.979 −5.959 −17.030 1.00 65.75 O ATOM 2243 CB MET B 36 30.289 −5.605 −17.389 1.00 53.08 C ATOM 2244 CG MET B 36 30.521 −5.432 −15.892 1.00 79.54 C ATOM 2245 SD MET B 36 30.994 −6.941 −15.011 1.00 69.83 S ATOM 2246 CE MET B 36 32.036 −7.739 −16.225 1.00 77.15 C ATOM 2247 N SER B 37 27.616 −5.219 −19.050 1.00 60.19 N ATOM 2248 CA SER B 37 26.336 −4.575 −19.339 1.00 49.26 C ATOM 2249 C SER B 37 25.237 −5.614 −19.537 1.00 56.99 C ATOM 2250 O SER B 37 24.068 −5.272 −19.715 1.00 51.07 O ATOM 2251 CB SER B 37 26.434 −3.717 −20.602 1.00 53.61 C ATOM 2252 OG SER B 37 27.490 −2.774 −20.529 1.00 58.61 O ATOM 2253 N LEU B 38 25.618 −6.886 −19.529 1.00 63.20 N ATOM 2254 CA LEU B 38 24.645 −7.951 −19.681 1.00 58.95 C ATOM 2255 C LEU B 38 24.163 −8.439 −18.317 1.00 58.92 C ATOM 2256 O LEU B 38 22.963 −8.445 −18.051 1.00 52.06 O ATOM 2257 CB LEU B 38 25.216 −9.103 −20.495 1.00 60.62 C ATOM 2258 CG LEU B 38 24.150 −9.871 −21.273 1.00 75.65 C ATOM 2259 CD1 LEU B 38 23.705 −9.065 −22.484 1.00 61.05 C ATOM 2260 CD2 LEU B 38 24.676 −11.223 −21.692 1.00 76.10 C ATOM 2261 N LEU B 39 25.093 −8.840 −17.450 1.00 58.52 N ATOM 2262 CA LEU B 39 24.718 −9.254 −16.094 1.00 74.76 C ATOM 2263 C LEU B 39 24.095 −8.090 −15.330 1.00 63.36 C ATOM 2264 O LEU B 39 23.247 −8.282 −14.456 1.00 59.24 O ATOM 2265 CB LEU B 39 25.902 −9.839 −15.301 1.00 74.03 C ATOM 2266 CG LEU B 39 26.230 −11.335 −15.454 1.00 93.97 C ATOM 2267 CD1 LEU B 39 26.624 −11.950 −14.105 1.00 76.81 C ATOM 2268 CD2 LEU B 39 25.070 −12.124 −16.066 1.00 74.37 C ATOM 2269 N MET B 40 24.515 −6.878 −15.667 1.00 62.09 N ATOM 2270 CA MET B 40 23.966 −5.708 −15.011 1.00 56.98 C ATOM 2271 C MET B 40 22.535 −5.511 −15.493 1.00 49.68 C ATOM 2272 O MET B 40 21.609 −5.408 −14.694 1.00 52.50 O ATOM 2273 CB MET B 40 24.824 −4.474 −15.288 1.00 46.31 C ATOM 2274 CG MET B 40 25.127 −3.644 −14.037 1.00 51.47 C ATOM 2275 SD MET B 40 26.046 −4.512 −12.733 1.00 71.14 S ATOM 2276 CE MET B 40 27.694 −4.565 −13.450 1.00 77.35 C ATOM 2277 N ALA B 41 22.353 −5.490 −16.805 1.00 39.02 N ATOM 2278 CA ALA B 41 21.021 −5.398 −17.373 1.00 42.96 C ATOM 2279 C ALA B 41 20.099 −6.479 −16.801 1.00 48.24 C ATOM 2280 O ALA B 41 18.884 −6.296 −16.718 1.00 39.23 O ATOM 2281 CB ALA B 41 21.094 −5.514 −18.875 1.00 36.52 C ATOM 2282 N LEU B 42 20.689 −7.602 −16.405 1.00 52.52 N ATOM 2283 CA LEU B 42 19.932 −8.733 −15.884 1.00 51.79 C ATOM 2284 C LEU B 42 19.400 −8.463 −14.483 1.00 52.03 C ATOM 2285 O LEU B 42 18.228 −8.713 −14.207 1.00 49.97 O ATOM 2286 CB LEU B 42 20.802 −9.986 −15.852 1.00 59.33 C ATOM 2287 CG LEU B 42 20.035 −11.300 −15.956 1.00 66.47 C ATOM 2288 CD1 LEU B 42 19.940 −11.694 −17.421 1.00 52.52 C ATOM 2289 CD2 LEU B 42 20.708 −12.393 −15.137 1.00 59.25 C ATOM 2290 N VAL B 43 20.266 −7.974 −13.597 1.00 47.11 N ATOM 2291 CA VAL B 43 19.849 −7.648 −12.235 1.00 43.68 C ATOM 2292 C VAL B 43 18.769 −6.574 −12.246 1.00 41.74 C ATOM 2293 O VAL B 43 17.761 −6.706 −11.566 1.00 48.21 O ATOM 2294 CB VAL B 43 21.024 −7.209 −11.325 1.00 41.47 C ATOM 2295 CG1 VAL B 43 22.078 −8.291 −11.268 1.00 46.55 C ATOM 2296 CG2 VAL B 43 21.632 −5.917 −11.813 1.00 47.55 C ATOM 2297 N VAL B 44 18.969 −5.520 −13.030 1.00 34.14 N ATOM 2298 CA VAL B 44 17.959 −4.483 −13.159 1.00 35.83 C ATOM 2299 C VAL B 44 16.606 −5.108 −13.514 1.00 44.98 C ATOM 2300 O VAL B 44 15.549 −4.656 −13.062 1.00 42.32 O ATOM 2301 CB VAL B 44 18.353 −3.446 −14.220 1.00 28.33 C ATOM 2302 CG1 VAL B 44 17.180 −2.524 −14.545 1.00 20.72 C ATOM 2303 CG2 VAL B 44 19.566 −2.652 −13.748 1.00 31.64 C ATOM 2304 N LEU B 45 16.655 −6.171 −14.307 1.00 49.30 N ATOM 2305 CA LEU B 45 15.453 −6.889 −14.717 1.00 52.52 C ATOM 2306 C LEU B 45 14.790 −7.645 −13.563 1.00 45.52 C ATOM 2307 O LEU B 45 13.577 −7.562 −13.379 1.00 41.75 O ATOM 2308 CB LEU B 45 15.782 −7.870 −15.838 1.00 54.51 C ATOM 2309 CG LEU B 45 14.581 −8.718 −16.251 1.00 56.80 C ATOM 2310 CD1 LEU B 45 13.548 −7.835 −16.926 1.00 49.11 C ATOM 2311 CD2 LEU B 45 14.998 −9.860 −17.154 1.00 43.93 C ATOM 2312 N LEU B 46 15.588 −8.409 −12.820 1.00 39.24 N ATOM 2313 CA LEU B 46 15.126 −9.060 −11.602 1.00 43.79 C ATOM 2314 C LEU B 46 14.451 −8.056 −10.673 1.00 50.22 C ATOM 2315 O LEU B 46 13.233 −8.078 −10.503 1.00 51.19 O ATOM 2316 CB LEU B 46 16.301 −9.701 −10.871 1.00 44.13 C ATOM 2317 CG LEU B 46 16.563 −11.165 −11.175 1.00 50.55 C ATOM 2318 CD1 LEU B 46 17.647 −11.707 −10.251 1.00 44.57 C ATOM 2319 CD2 LEU B 46 15.267 −11.939 −10.998 1.00 60.03 C ATOM 2320 N ILE B 47 15.258 −7.177 −10.080 1.00 43.53 N ATOM 2321 CA ILE B 47 14.767 −6.119 −9.204 1.00 48.12 C ATOM 2322 C ILE B 47 13.527 −5.417 −9.741 1.00 41.51 C ATOM 2323 O ILE B 47 12.555 −5.240 −9.011 1.00 42.93 O ATOM 2324 CB ILE B 47 15.843 −5.036 −8.940 1.00 49.99 C ATOM 2325 CG1 ILE B 47 17.100 −5.653 −8.337 1.00 39.53 C ATOM 2326 CG2 ILE B 47 15.296 −3.939 −8.023 1.00 34.66 C ATOM 2327 CD1 ILE B 47 18.296 −4.738 −8.403 1.00 35.38 C ATOM 2328 N VAL B 48 13.554 −4.994 −11.001 1.00 33.39 N ATOM 2329 CA VAL B 48 12.411 −4.241 −11.505 1.00 40.39 C ATOM 2330 C VAL B 48 11.171 −5.097 −11.699 1.00 45.70 C ATOM 2331 O VAL B 48 10.068 −4.688 −11.331 1.00 57.27 O ATOM 2332 CB VAL B 48 12.701 −3.460 −12.783 1.00 36.27 C ATOM 2333 CG1 VAL B 48 11.399 −2.885 −13.322 1.00 28.81 C ATOM 2334 CG2 VAL B 48 13.698 −2.333 −12.503 1.00 34.41 C ATOM 2335 N ALA B 49 11.343 −6.286 −12.262 1.00 44.35 N ATOM 2336 CA ALA B 49 10.201 −7.168 −12.496 1.00 49.26 C ATOM 2337 C ALA B 49 9.562 −7.669 −11.190 1.00 50.96 C ATOM 2338 O ALA B 49 8.342 −7.591 −11.005 1.00 43.23 O ATOM 2339 CB ALA B 49 10.599 −8.341 −13.385 1.00 32.52 C ATOM 2340 N GLY B 50 10.391 −8.181 −10.287 1.00 44.01 N ATOM 2341 CA GLY B 50 9.899 −8.779 −9.060 1.00 48.90 C ATOM 2342 C GLY B 50 9.195 −7.794 −8.145 1.00 49.18 C ATOM 2343 O GLY B 50 8.241 −8.138 −7.453 1.00 48.56 O ATOM 2344 N ASN B 51 9.665 −6.557 −8.140 1.00 47.93 N ATOM 2345 CA ASN B 51 9.116 −5.569 −7.235 1.00 44.33 C ATOM 2346 C ASN B 51 7.899 −4.894 −7.819 1.00 47.36 C ATOM 2347 O ASN B 51 7.081 −4.343 −7.088 1.00 55.88 O ATOM 2348 CB ASN B 51 10.173 −4.538 −6.857 1.00 44.74 C ATOM 2349 CG ASN B 51 11.077 −5.026 −5.751 1.00 48.93 C ATOM 2350 OD1 ASN B 51 10.668 −5.095 −4.586 1.00 49.15 O ATOM 2351 ND2 ASN B 51 12.315 −5.376 −6.104 1.00 44.73 N ATOM 2352 N VAL B 52 7.785 −4.926 −9.139 1.00 41.94 N ATOM 2353 CA VAL B 52 6.594 −4.403 −9.787 1.00 46.77 C ATOM 2354 C VAL B 52 5.500 −5.455 −9.644 1.00 49.35 C ATOM 2355 O VAL B 52 4.314 −5.137 −9.563 1.00 46.91 O ATOM 2356 CB VAL B 52 6.865 −4.064 −11.263 1.00 38.84 C ATOM 2357 CG1 VAL B 52 5.571 −3.939 −12.036 1.00 22.72 C ATOM 2358 CG2 VAL B 52 7.669 −2.780 −11.355 1.00 38.08 C ATOM 2359 N LEU B 53 5.932 −6.710 −9.573 1.00 48.26 N ATOM 2360 CA LEU B 53 5.049 −7.850 −9.376 1.00 46.69 C ATOM 2361 C LEU B 53 4.378 −7.776 −8.012 1.00 56.49 C ATOM 2362 O LEU B 53 3.160 −7.915 −7.891 1.00 55.54 O ATOM 2363 CB LEU B 53 5.865 −9.135 −9.467 1.00 55.12 C ATOM 2364 CG LEU B 53 5.262 −10.279 −10.273 1.00 68.12 C ATOM 2365 CD1 LEU B 53 4.778 −9.773 −11.622 1.00 55.24 C ATOM 2366 CD2 LEU B 53 6.293 −11.376 −10.456 1.00 79.59 C ATOM 2367 N VAL B 54 5.192 −7.568 −6.982 1.00 61.13 N ATOM 2368 CA VAL B 54 4.704 −7.394 −5.621 1.00 49.52 C ATOM 2369 C VAL B 54 3.686 −6.258 −5.530 1.00 50.76 C ATOM 2370 O VAL B 54 2.550 −6.470 −5.118 1.00 51.56 O ATOM 2371 CB VAL B 54 5.865 −7.113 −4.655 1.00 44.36 C ATOM 2372 CG1 VAL B 54 5.337 −6.715 −3.283 1.00 49.18 C ATOM 2373 CG2 VAL B 54 6.772 −8.329 −4.554 1.00 49.20 C ATOM 2374 N ILE B 55 4.096 −5.057 −5.923 1.00 48.29 N ATOM 2375 CA ILE B 55 3.226 −3.889 −5.844 1.00 48.41 C ATOM 2376 C ILE B 55 1.913 −4.111 −6.581 1.00 55.18 C ATOM 2377 O ILE B 55 0.859 −3.678 −6.121 1.00 68.61 O ATOM 2378 CB ILE B 55 3.898 −2.630 −6.410 1.00 45.84 C ATOM 2379 CG1 ILE B 55 5.025 −2.164 −5.487 1.00 45.38 C ATOM 2380 CG2 ILE B 55 2.878 −1.528 −6.576 1.00 38.25 C ATOM 2381 CD1 ILE B 55 6.055 −1.278 −6.175 1.00 39.92 C ATOM 2382 N ALA B 56 1.969 −4.790 −7.719 1.00 50.12 N ATOM 2383 CA ALA B 56 0.759 −5.044 −8.487 1.00 49.96 C ATOM 2384 C ALA B 56 −0.101 −6.137 −7.859 1.00 55.20 C ATOM 2385 O ALA B 56 −1.322 −6.021 −7.828 1.00 60.94 O ATOM 2386 CB ALA B 56 1.101 −5.391 −9.915 1.00 38.35 C ATOM 2387 N ALA B 57 0.535 −7.193 −7.358 1.00 52.20 N ATOM 2388 CA ALA B 57 −0.190 −8.296 −6.726 1.00 64.35 C ATOM 2389 C ALA B 57 −1.006 −7.817 −5.527 1.00 74.92 C ATOM 2390 O ALA B 57 −2.169 −8.192 −5.359 1.00 78.24 O ATOM 2391 CB ALA B 57 0.771 −9.394 −6.299 1.00 63.84 C ATOM 2392 N ILE B 58 −0.381 −6.995 −4.691 1.00 72.21 N ATOM 2393 CA ILE B 58 −1.051 −6.424 −3.533 1.00 68.16 C ATOM 2394 C ILE B 58 −2.139 −5.470 −4.001 1.00 66.75 C ATOM 2395 O ILE B 58 −3.223 −5.423 −3.424 1.00 81.83 O ATOM 2396 CB ILE B 58 −0.048 −5.706 −2.607 1.00 59.43 C ATOM 2397 CG1 ILE B 58 0.888 −6.728 −1.969 1.00 50.22 C ATOM 2398 CG2 ILE B 58 −0.763 −4.914 −1.519 1.00 50.40 C ATOM 2399 CD1 ILE B 58 2.031 −6.101 −1.210 1.00 60.36 C ATOM 2400 N GLY B 59 −1.851 −4.726 −5.063 1.00 62.24 N ATOM 2401 CA GLY B 59 −2.830 −3.825 −5.643 1.00 81.36 C ATOM 2402 C GLY B 59 −4.028 −4.546 −6.243 1.00 88.64 C ATOM 2403 O GLY B 59 −5.129 −3.996 −6.306 1.00 81.11 O ATOM 2404 N SER B 60 −3.812 −5.783 −6.682 1.00 88.58 N ATOM 2405 CA SER B 60 −4.862 −6.565 −7.332 1.00 93.29 C ATOM 2406 C SER B 60 −5.826 −7.177 −6.319 1.00 91.37 C ATOM 2407 O SER B 60 −6.997 −6.804 −6.263 1.00 110.99 O ATOM 2408 CB SER B 60 −4.257 −7.657 −8.223 1.00 72.53 C ATOM 2409 OG SER B 60 −3.527 −7.086 −9.295 1.00 70.64 O ATOM 2410 N THR B 61 −5.332 −8.119 −5.523 1.00 86.94 N ATOM 2411 CA THR B 61 −6.149 −8.765 −4.500 1.00 102.13 C ATOM 2412 C THR B 61 −6.273 −7.879 −3.262 1.00 113.92 C ATOM 2413 O THR B 61 −5.268 −7.375 −2.752 1.00 113.13 O ATOM 2414 CB THR B 61 −5.529 −10.107 −4.057 1.00 107.16 C ATOM 2415 OG1 THR B 61 −4.709 −10.637 −5.108 1.00 103.36 O ATOM 2416 CG2 THR B 61 −6.619 −11.112 −3.682 1.00 104.62 C ATOM 2417 N GLN B 62 −7.497 −7.686 −2.777 1.00 111.63 N ATOM 2418 CA GLN B 62 −7.688 −6.999 −1.502 1.00 113.97 C ATOM 2419 C GLN B 62 −7.446 −8.003 −0.387 1.00 106.34 C ATOM 2420 O GLN B 62 −7.163 −7.631 0.753 1.00 91.97 O ATOM 2421 CB GLN B 62 −9.099 −6.439 −1.380 1.00 118.58 C ATOM 2422 CG GLN B 62 −9.664 −5.890 −2.665 1.00 121.46 C ATOM 2423 CD GLN B 62 −11.155 −6.117 −2.754 1.00 101.14 C ATOM 2424 OE1 GLN B 62 −11.777 −6.579 −1.794 1.00 84.46 O ATOM 2425 NE2 GLN B 62 −11.739 −5.807 −3.908 1.00 95.67 N ATOM 2426 N ARG B 63 −7.578 −9.282 −0.729 1.00 102.88 N ATOM 2427 CA ARG B 63 −7.207 −10.353 0.177 1.00 97.41 C ATOM 2428 C ARG B 63 −5.760 −10.139 0.611 1.00 104.74 C ATOM 2429 O ARG B 63 −5.431 −10.213 1.798 1.00 90.21 O ATOM 2430 CB ARG B 63 −7.352 −11.705 −0.511 1.00 85.82 C ATOM 2431 CG ARG B 63 −7.031 −12.868 0.396 1.00 107.12 C ATOM 2432 CD ARG B 63 −6.779 −14.136 −0.385 1.00 113.27 C ATOM 2433 NE ARG B 63 −6.369 −15.220 0.502 1.00 131.42 N ATOM 2434 CZ ARG B 63 −6.090 −16.455 0.098 1.00 143.25 C ATOM 2435 NH1 ARG B 63 −6.172 −16.767 −1.188 1.00 148.48 N ATOM 2436 NH2 ARG B 63 −5.722 −17.377 0.979 1.00 137.33 N ATOM 2437 N LEU B 64 −4.901 −9.861 −0.366 1.00 106.61 N ATOM 2438 CA LEU B 64 −3.511 −9.513 −0.099 1.00 94.75 C ATOM 2439 C LEU B 64 −3.369 −8.114 0.519 1.00 89.75 C ATOM 2440 O LEU B 64 −2.310 −7.765 1.036 1.00 80.47 O ATOM 2441 CB LEU B 64 −2.673 −9.613 −1.379 1.00 90.70 C ATOM 2442 CG LEU B 64 −2.000 −10.949 −1.716 1.00 94.68 C ATOM 2443 CD1 LEU B 64 −1.151 −10.828 −2.982 1.00 85.00 C ATOM 2444 CD2 LEU B 64 −1.148 −11.432 −0.555 1.00 75.29 C ATOM 2445 N GLN B 65 −4.423 −7.307 0.465 1.00 87.14 N ATOM 2446 CA GLN B 65 −4.360 −5.985 1.086 1.00 84.39 C ATOM 2447 C GLN B 65 −4.630 −6.023 2.586 1.00 87.05 C ATOM 2448 O GLN B 65 −5.761 −5.843 3.038 1.00 88.26 O ATOM 2449 CB GLN B 65 −5.282 −4.984 0.391 1.00 93.23 C ATOM 2450 CG GLN B 65 −4.540 −3.980 −0.469 1.00 83.58 C ATOM 2451 CD GLN B 65 −5.472 −3.055 −1.222 1.00 97.96 C ATOM 2452 OE1 GLN B 65 −6.677 −3.301 −1.307 1.00 109.30 O ATOM 2453 NE2 GLN B 65 −4.917 −1.984 −1.780 1.00 81.55 N ATOM 2454 N THR B 66 −3.568 −6.281 3.341 1.00 76.47 N ATOM 2455 CA THR B 66 −3.577 −6.171 4.788 1.00 44.72 C ATOM 2456 C THR B 66 −2.803 −4.909 5.109 1.00 50.95 C ATOM 2457 O THR B 66 −2.424 −4.173 4.200 1.00 71.88 O ATOM 2458 CB THR B 66 −2.839 −7.341 5.418 1.00 53.39 C ATOM 2459 OG1 THR B 66 −1.448 −7.235 5.103 1.00 56.75 O ATOM 2460 CG2 THR B 66 −3.372 −8.659 4.881 1.00 46.46 C ATOM 2461 N LEU B 67 −2.565 −4.646 6.388 1.00 52.71 N ATOM 2462 CA LEU B 67 −1.746 −3.502 6.780 1.00 49.66 C ATOM 2463 C LEU B 67 −0.286 −3.833 6.540 1.00 53.48 C ATOM 2464 O LEU B 67 0.467 −3.034 5.983 1.00 52.47 O ATOM 2465 CB LEU B 67 −1.936 −3.178 8.261 1.00 56.05 C ATOM 2466 CG LEU B 67 −3.098 −2.281 8.664 1.00 45.36 C ATOM 2467 CD1 LEU B 67 −2.863 −1.801 10.086 1.00 56.88 C ATOM 2468 CD2 LEU B 67 −3.214 −1.109 7.710 1.00 42.61 C ATOM 2469 N THR B 68 0.101 −5.024 6.985 1.00 48.72 N ATOM 2470 CA THR B 68 1.458 −5.517 6.823 1.00 42.69 C ATOM 2471 C THR B 68 1.927 −5.319 5.403 1.00 41.03 C ATOM 2472 O THR B 68 3.062 −4.912 5.172 1.00 48.54 O ATOM 2473 CB THR B 68 1.554 −7.013 7.170 1.00 51.90 C ATOM 2474 OG1 THR B 68 1.404 −7.191 8.585 1.00 60.76 O ATOM 2475 CG2 THR B 68 2.892 −7.589 6.725 1.00 42.57 C ATOM 2476 N ASN B 69 1.045 −5.603 4.455 1.00 39.11 N ATOM 2477 CA ASN B 69 1.398 −5.536 3.045 1.00 44.58 C ATOM 2478 C ASN B 69 1.478 −4.109 2.528 1.00 43.73 C ATOM 2479 O ASN B 69 2.077 −3.853 1.482 1.00 45.50 O ATOM 2480 CB ASN B 69 0.427 −6.367 2.210 1.00 56.62 C ATOM 2481 CG ASN B 69 0.622 −7.849 2.414 1.00 49.98 C ATOM 2482 OD1 ASN B 69 1.619 −8.277 2.989 1.00 54.00 O ATOM 2483 ND2 ASN B 69 −0.324 −8.640 1.946 1.00 61.34 N ATOM 2484 N LEU B 70 0.873 −3.187 3.265 1.00 37.97 N ATOM 2485 CA LEU B 70 1.040 −1.769 2.985 1.00 43.30 C ATOM 2486 C LEU B 70 2.480 −1.334 3.243 1.00 38.70 C ATOM 2487 O LEU B 70 3.064 −0.581 2.455 1.00 29.24 O ATOM 2488 CB LEU B 70 0.081 −0.939 3.834 1.00 53.28 C ATOM 2489 CG LEU B 70 −1.347 −0.967 3.308 1.00 48.55 C ATOM 2490 CD1 LEU B 70 −2.190 0.083 4.010 1.00 45.61 C ATOM 2491 CD2 LEU B 70 −1.311 −0.743 1.808 1.00 32.37 C ATOM 2492 N PHE B 71 3.049 −1.818 4.343 1.00 37.13 N ATOM 2493 CA PHE B 71 4.453 −1.547 4.655 1.00 45.05 C ATOM 2494 C PHE B 71 5.405 −2.276 3.705 1.00 37.96 C ATOM 2495 O PHE B 71 6.486 −1.771 3.374 1.00 31.22 O ATOM 2496 CB PHE B 71 4.771 −1.872 6.120 1.00 40.28 C ATOM 2497 CG PHE B 71 3.952 −1.080 7.095 1.00 37.11 C ATOM 2498 CD1 PHE B 71 3.763 0.278 6.909 1.00 38.42 C ATOM 2499 CD2 PHE B 71 3.365 −1.692 8.192 1.00 42.01 C ATOM 2500 CE1 PHE B 71 2.991 1.016 7.796 1.00 44.05 C ATOM 2501 CE2 PHE B 71 2.597 −0.961 9.087 1.00 35.22 C ATOM 2502 CZ PHE B 71 2.409 0.396 8.890 1.00 35.08 C ATOM 2503 N ILE B 72 4.979 −3.455 3.257 1.00 41.92 N ATOM 2504 CA ILE B 72 5.702 −4.229 2.247 1.00 40.01 C ATOM 2505 C ILE B 72 5.761 −3.498 0.902 1.00 31.05 C ATOM 2506 O ILE B 72 6.753 −3.558 0.192 1.00 30.14 O ATOM 2507 CB ILE B 72 5.033 −5.593 2.039 1.00 41.02 C ATOM 2508 CG1 ILE B 72 5.252 −6.479 3.264 1.00 42.22 C ATOM 2509 CG2 ILE B 72 5.570 −6.273 0.802 1.00 41.85 C ATOM 2510 CD1 ILE B 72 6.570 −7.163 3.282 1.00 40.80 C ATOM 2511 N THR B 73 4.685 −2.815 0.551 1.00 31.86 N ATOM 2512 CA THR B 73 4.678 −2.022 −0.662 1.00 34.12 C ATOM 2513 C THR B 73 5.704 −0.905 −0.561 1.00 32.79 C ATOM 2514 O THR B 73 6.408 −0.600 −1.519 1.00 30.72 O ATOM 2515 CB THR B 73 3.293 −1.415 −0.939 1.00 37.75 C ATOM 2516 OG1 THR B 73 2.352 −2.465 −1.189 1.00 35.86 O ATOM 2517 CG2 THR B 73 3.350 −0.502 −2.153 1.00 36.94 C ATOM 2518 N SER B 74 5.778 −0.296 0.613 1.00 37.11 N ATOM 2519 CA SER B 74 6.711 0.793 0.859 1.00 34.77 C ATOM 2520 C SER B 74 8.114 0.276 0.613 1.00 34.92 C ATOM 2521 O SER B 74 8.948 0.936 −0.008 1.00 33.69 O ATOM 2522 CB SER B 74 6.566 1.291 2.297 1.00 32.39 C ATOM 2523 OG SER B 74 7.507 2.301 2.586 1.00 40.13 O ATOM 2524 N LEU B 75 8.353 −0.930 1.106 1.00 36.86 N ATOM 2525 CA LEU B 75 9.599 −1.638 0.886 1.00 28.84 C ATOM 2526 C LEU B 75 9.837 −1.875 −0.607 1.00 33.13 C ATOM 2527 O LEU B 75 10.937 −1.637 −1.106 1.00 39.30 O ATOM 2528 CB LEU B 75 9.538 −2.969 1.620 1.00 32.88 C ATOM 2529 CG LEU B 75 10.786 −3.413 2.354 1.00 33.06 C ATOM 2530 CD1 LEU B 75 11.353 −2.244 3.120 1.00 33.18 C ATOM 2531 CD2 LEU B 75 10.438 −4.572 3.273 1.00 36.25 C ATOM 2532 N ALA B 76 8.808 −2.345 −1.313 1.00 30.13 N ATOM 2533 CA ALA B 76 8.895 −2.580 −2.758 1.00 33.92 C ATOM 2534 C ALA B 76 9.292 −1.321 −3.531 1.00 36.72 C ATOM 2535 O ALA B 76 10.150 −1.369 −4.410 1.00 40.26 O ATOM 2536 CB ALA B 76 7.585 −3.142 −3.298 1.00 31.56 C ATOM 2537 N CYS B 77 8.669 −0.196 −3.200 1.00 33.85 N ATOM 2538 CA CYS B 77 8.981 1.061 −3.862 1.00 28.40 C ATOM 2539 C CYS B 77 10.425 1.487 −3.663 1.00 27.87 C ATOM 2540 O CYS B 77 11.037 2.021 −4.579 1.00 27.46 O ATOM 2541 CB CYS B 77 8.048 2.170 −3.384 1.00 21.53 C ATOM 2542 SG CYS B 77 6.368 2.029 −4.017 1.00 51.06 S ATOM 2543 N ALA B 78 10.971 1.271 −2.472 1.00 26.71 N ATOM 2544 CA ALA B 78 12.368 1.625 −2.250 1.00 32.36 C ATOM 2545 C ALA B 78 13.305 0.716 −3.048 1.00 34.78 C ATOM 2546 O ALA B 78 14.376 1.143 −3.454 1.00 38.39 O ATOM 2547 CB ALA B 78 12.717 1.603 −0.778 1.00 26.78 C ATOM 2548 N ASP B 79 12.896 −0.529 −3.282 1.00 33.95 N ATOM 2549 CA ASP B 79 13.678 −1.425 −4.129 1.00 33.38 C ATOM 2550 C ASP B 79 13.545 −1.037 −5.610 1.00 35.56 C ATOM 2551 O ASP B 79 14.478 −1.208 −6.397 1.00 34.90 O ATOM 2552 CB ASP B 79 13.294 −2.884 −3.882 1.00 30.44 C ATOM 2553 CG ASP B 79 13.618 −3.342 −2.454 1.00 60.19 C ATOM 2554 OD1 ASP B 79 14.679 −2.930 −1.915 1.00 51.01 O ATOM 2555 OD2 ASP B 79 12.812 −4.116 −1.873 1.00 63.48 O ATOM 2556 N LEU B 80 12.395 −0.479 −5.971 1.00 26.75 N ATOM 2557 CA LEU B 80 12.155 −0.022 −7.330 1.00 28.95 C ATOM 2558 C LEU B 80 13.040 1.165 −7.705 1.00 34.79 C ATOM 2559 O LEU B 80 13.729 1.146 −8.726 1.00 40.98 O ATOM 2560 CB LEU B 80 10.687 0.332 −7.521 1.00 37.91 C ATOM 2561 CG LEU B 80 10.135 0.051 −8.917 1.00 40.15 C ATOM 2562 CD1 LEU B 80 10.313 −1.419 −9.283 1.00 38.78 C ATOM 2563 CD2 LEU B 80 8.678 0.451 −8.995 1.00 28.80 C ATOM 2564 N VAL B 81 13.018 2.205 −6.886 1.00 39.16 N ATOM 2565 CA VAL B 81 13.944 3.317 −7.069 1.00 41.38 C ATOM 2566 C VAL B 81 15.368 2.799 −7.331 1.00 35.74 C ATOM 2567 O VAL B 81 16.044 3.271 −8.238 1.00 37.28 O ATOM 2568 CB VAL B 81 13.932 4.290 −5.855 1.00 40.58 C ATOM 2569 CG1 VAL B 81 14.881 5.445 −6.089 1.00 31.34 C ATOM 2570 CG2 VAL B 81 12.518 4.824 −5.600 1.00 32.21 C ATOM 2571 N VAL B 82 15.816 1.817 −6.553 1.00 27.77 N ATOM 2572 CA VAL B 82 17.155 1.253 −6.730 1.00 34.85 C ATOM 2573 C VAL B 82 17.349 0.555 −8.086 1.00 44.70 C ATOM 2574 O VAL B 82 18.363 0.768 −8.770 1.00 35.87 O ATOM 2575 CB VAL B 82 17.523 0.270 −5.598 1.00 28.58 C ATOM 2576 CG1 VAL B 82 18.834 −0.462 −5.912 1.00 25.88 C ATOM 2577 CG2 VAL B 82 17.626 1.003 −4.292 1.00 25.57 C ATOM 2578 N GLY B 83 16.385 −0.282 −8.468 1.00 37.50 N ATOM 2579 CA GLY B 83 16.448 −0.966 −9.747 1.00 41.11 C ATOM 2580 C GLY B 83 16.366 −0.015 −10.933 1.00 35.83 C ATOM 2581 O GLY B 83 16.933 −0.276 −11.993 1.00 25.50 O ATOM 2582 N LEU B 84 15.658 1.094 −10.742 1.00 33.48 N ATOM 2583 CA LEU B 84 15.450 2.074 −11.800 1.00 34.52 C ATOM 2584 C LEU B 84 16.506 3.183 −11.835 1.00 38.42 C ATOM 2585 O LEU B 84 16.931 3.593 −12.915 1.00 41.82 O ATOM 2586 CB LEU B 84 14.062 2.708 −11.680 1.00 38.40 C ATOM 2587 CG LEU B 84 12.832 1.868 −12.011 1.00 34.14 C ATOM 2588 CD1 LEU B 84 11.606 2.750 −11.945 1.00 21.05 C ATOM 2589 CD2 LEU B 84 12.976 1.226 −13.379 1.00 29.95 C ATOM 2590 N LEU B 85 16.918 3.680 −10.672 1.00 32.76 N ATOM 2591 CA LEU B 85 17.874 4.788 −10.632 1.00 30.47 C ATOM 2592 C LEU B 85 19.248 4.429 −10.063 1.00 33.38 C ATOM 2593 O LEU B 85 20.268 4.643 −10.715 1.00 36.10 O ATOM 2594 CB LEU B 85 17.278 5.985 −9.887 1.00 34.29 C ATOM 2595 CG LEU B 85 16.057 6.551 −10.611 1.00 34.40 C ATOM 2596 CD1 LEU B 85 15.509 7.793 −9.949 1.00 31.74 C ATOM 2597 CD2 LEU B 85 16.442 6.852 −12.040 1.00 42.40 C ATOM 2598 N VAL B 86 19.281 3.875 −8.857 1.00 30.60 N ATOM 2599 CA VAL B 86 20.562 3.618 −8.211 1.00 33.48 C ATOM 2600 C VAL B 86 21.481 2.679 −9.010 1.00 30.28 C ATOM 2601 O VAL B 86 22.579 3.070 −9.368 1.00 31.55 O ATOM 2602 CB VAL B 86 20.388 3.115 −6.770 1.00 26.48 C ATOM 2603 CG1 VAL B 86 21.734 3.074 −6.059 1.00 27.28 C ATOM 2604 CG2 VAL B 86 19.438 4.012 −6.037 1.00 26.79 C ATOM 2605 N VAL B 87 21.032 1.459 −9.296 1.00 34.56 N ATOM 2606 CA VAL B 87 21.886 0.462 −9.954 1.00 35.58 C ATOM 2607 C VAL B 87 22.273 0.837 −11.388 1.00 39.16 C ATOM 2608 O VAL B 87 23.428 0.675 −11.772 1.00 42.29 O ATOM 2609 CB VAL B 87 21.275 −0.969 −9.939 1.00 35.29 C ATOM 2610 CG1 VAL B 87 21.891 −1.822 −11.046 1.00 25.30 C ATOM 2611 CG2 VAL B 87 21.476 −1.625 −8.578 1.00 29.44 C ATOM 2612 N PRO B 88 21.307 1.320 −12.190 1.00 35.02 N ATOM 2613 CA PRO B 88 21.637 1.830 −13.528 1.00 33.34 C ATOM 2614 C PRO B 88 22.849 2.783 −13.564 1.00 37.40 C ATOM 2615 O PRO B 88 23.840 2.457 −14.213 1.00 34.67 O ATOM 2616 CB PRO B 88 20.350 2.539 −13.951 1.00 26.86 C ATOM 2617 CG PRO B 88 19.275 1.711 −13.305 1.00 29.33 C ATOM 2618 CD PRO B 88 19.849 1.197 −11.995 1.00 33.93 C ATOM 2619 N PHE B 89 22.785 3.929 −12.891 1.00 33.65 N ATOM 2620 CA PHE B 89 23.927 4.841 −12.883 1.00 31.24 C ATOM 2621 C PHE B 89 25.144 4.184 −12.218 1.00 36.97 C ATOM 2622 O PHE B 89 26.290 4.434 −12.602 1.00 33.35 O ATOM 2623 CB PHE B 89 23.613 6.098 −12.091 1.00 32.08 C ATOM 2624 CG PHE B 89 22.688 7.058 −12.766 1.00 26.57 C ATOM 2625 CD1 PHE B 89 23.178 8.239 −13.316 1.00 30.15 C ATOM 2626 CD2 PHE B 89 21.321 6.826 −12.782 1.00 30.09 C ATOM 2627 CE1 PHE B 89 22.321 9.171 −13.896 1.00 31.45 C ATOM 2628 CE2 PHE B 89 20.450 7.737 −13.366 1.00 26.89 C ATOM 2629 CZ PHE B 89 20.950 8.916 −13.923 1.00 35.92 C ATOM 2630 N GLY B 90 24.895 3.375 −11.192 1.00 31.65 N ATOM 2631 CA GLY B 90 25.963 2.717 −10.462 1.00 27.50 C ATOM 2632 C GLY B 90 26.708 1.711 −11.317 1.00 35.94 C ATOM 2633 O GLY B 90 27.901 1.492 −11.149 1.00 27.01 O ATOM 2634 N ALA B 91 25.987 1.095 −12.245 1.00 43.48 N ATOM 2635 CA ALA B 91 26.577 0.185 −13.213 1.00 41.13 C ATOM 2636 C ALA B 91 27.630 0.883 −14.098 1.00 38.74 C ATOM 2637 O ALA B 91 28.755 0.398 −14.236 1.00 34.38 O ATOM 2638 CB ALA B 91 25.486 −0.434 −14.062 1.00 33.13 C ATOM 2639 N THR B 92 27.259 2.015 −14.695 1.00 28.35 N ATOM 2640 CA THR B 92 28.180 2.785 −15.524 1.00 26.92 C ATOM 2641 C THR B 92 29.466 3.085 −14.759 1.00 34.07 C ATOM 2642 O THR B 92 30.560 2.964 −15.297 1.00 34.06 O ATOM 2643 CB THR B 92 27.554 4.122 −16.052 1.00 34.13 C ATOM 2644 OG1 THR B 92 27.572 5.137 −15.033 1.00 33.42 O ATOM 2645 CG2 THR B 92 26.137 3.903 −16.527 1.00 29.55 C ATOM 2646 N LEU B 93 29.327 3.466 −13.496 1.00 34.88 N ATOM 2647 CA LEU B 93 30.483 3.767 −12.666 1.00 35.78 C ATOM 2648 C LEU B 93 31.418 2.565 −12.502 1.00 31.13 C ATOM 2649 O LEU B 93 32.633 2.719 −12.431 1.00 34.51 O ATOM 2650 CB LEU B 93 30.024 4.274 −11.298 1.00 35.00 C ATOM 2651 CG LEU B 93 31.058 4.775 −10.289 1.00 28.87 C ATOM 2652 CD1 LEU B 93 32.032 5.766 −10.917 1.00 19.28 C ATOM 2653 CD2 LEU B 93 30.308 5.426 −9.147 1.00 31.84 C ATOM 2654 N VAL B 94 30.856 1.369 −12.427 1.00 33.68 N ATOM 2655 CA VAL B 94 31.674 0.194 −12.168 1.00 42.30 C ATOM 2656 C VAL B 94 32.275 −0.351 −13.463 1.00 53.81 C ATOM 2657 O VAL B 94 33.399 −0.865 −13.473 1.00 47.71 O ATOM 2658 CB VAL B 94 30.889 −0.917 −11.446 1.00 44.56 C ATOM 2659 CG1 VAL B 94 31.857 −1.913 −10.841 1.00 38.11 C ATOM 2660 CG2 VAL B 94 30.010 −0.321 −10.359 1.00 50.06 C ATOM 2661 N VAL B 95 31.527 −0.226 −14.555 1.00 40.59 N ATOM 2662 CA VAL B 95 32.018 −0.648 −15.858 1.00 43.57 C ATOM 2663 C VAL B 95 33.120 0.275 −16.405 1.00 46.90 C ATOM 2664 O VAL B 95 34.093 −0.194 −16.986 1.00 52.48 O ATOM 2665 CB VAL B 95 30.870 −0.768 −16.879 1.00 38.40 C ATOM 2666 CG1 VAL B 95 31.416 −1.095 −18.246 1.00 56.62 C ATOM 2667 CG2 VAL B 95 29.877 −1.836 −16.436 1.00 53.81 C ATOM 2668 N ARG B 96 32.978 1.581 −16.203 1.00 41.13 N ATOM 2669 CA ARG B 96 33.899 2.543 −16.796 1.00 31.67 C ATOM 2670 C ARG B 96 34.944 3.116 −15.851 1.00 36.55 C ATOM 2671 O ARG B 96 35.901 3.755 −16.297 1.00 45.67 O ATOM 2672 CB ARG B 96 33.135 3.683 −17.455 1.00 30.76 C ATOM 2673 CG ARG B 96 32.608 3.335 −18.853 1.00 54.47 C ATOM 2674 CD ARG B 96 33.752 3.100 −19.845 1.00 44.11 C ATOM 2675 NE ARG B 96 34.588 4.286 −20.026 1.00 37.39 N ATOM 2676 CZ ARG B 96 34.200 5.367 −20.703 1.00 42.82 C ATOM 2677 NH1 ARG B 96 32.990 5.408 −21.253 1.00 26.41 N ATOM 2678 NH2 ARG B 96 35.019 6.407 −20.824 1.00 32.70 N ATOM 2679 N GLY B 97 34.767 2.890 −14.556 1.00 33.05 N ATOM 2680 CA GLY B 97 35.631 3.484 −13.557 1.00 25.63 C ATOM 2681 C GLY B 97 35.668 5.007 −13.587 1.00 34.01 C ATOM 2682 O GLY B 97 36.683 5.599 −13.229 1.00 44.61 O ATOM 2683 N THR B 98 34.578 5.644 −14.021 1.00 25.76 N ATOM 2684 CA THR B 98 34.487 7.104 −14.044 1.00 27.04 C ATOM 2685 C THR B 98 33.032 7.473 −13.984 1.00 30.83 C ATOM 2686 O THR B 98 32.168 6.626 −14.199 1.00 34.86 O ATOM 2687 CB THR B 98 35.035 7.739 −15.347 1.00 31.16 C ATOM 2688 OG1 THR B 98 35.961 6.853 −15.971 1.00 39.15 O ATOM 2689 CG2 THR B 98 35.705 9.078 −15.068 1.00 21.21 C ATOM 2690 N TRP B 99 32.767 8.748 −13.719 1.00 23.92 N ATOM 2691 CA TRP B 99 31.411 9.257 −13.680 1.00 21.86 C ATOM 2692 C TRP B 99 31.143 10.058 −14.940 1.00 25.43 C ATOM 2693 O TRP B 99 31.815 11.055 −15.191 1.00 27.16 O ATOM 2694 CB TRP B 99 31.183 10.102 −12.426 1.00 19.01 O ATOM 2695 CG TRP B 99 29.743 10.435 −12.193 1.00 21.61 C ATOM 2696 CD1 TRP B 99 29.163 11.656 −12.324 1.00 21.40 C ATOM 2697 CD2 TRP B 99 28.697 9.532 −11.801 1.00 16.86 C ATOM 2698 NE1 TRP B 99 27.826 11.579 −12.024 1.00 27.38 N ATOM 2699 CE2 TRP B 99 27.514 10.288 −11.696 1.00 23.16 C ATOM 2700 CE3 TRP B 99 28.649 8.163 −11.518 1.00 19.92 C ATOM 2701 CZ2 TRP B 99 26.290 9.720 −11.336 1.00 19.09 C ATOM 2702 CZ3 TRP B 99 27.436 7.597 −11.147 1.00 18.27 C ATOM 2703 CH2 TRP B 99 26.274 8.373 −11.067 1.00 21.87 C ATOM 2704 N LEU B 100 30.162 9.617 −15.731 1.00 24.59 N ATOM 2705 CA LEU B 100 29.878 10.249 −17.022 1.00 25.59 C ATOM 2706 C LEU B 100 28.863 11.378 −16.925 1.00 28.75 C ATOM 2707 O LEU B 100 28.643 12.101 −17.897 1.00 27.21 O ATOM 2708 CB LEU B 100 29.326 9.239 −18.032 1.00 28.56 C ATOM 2709 CG LEU B 100 29.990 7.945 −18.520 1.00 34.85 C ATOM 2710 CD1 LEU B 100 29.339 7.582 −19.841 1.00 33.91 C ATOM 2711 CD2 LEU B 100 31.503 8.054 −18.694 1.00 32.67 C ATOM 2712 N TRP B 101 28.242 11.538 −15.764 1.00 26.88 N ATOM 2713 CA TRP B 101 26.988 12.275 −15.714 1.00 24.26 C ATOM 2714 C TRP B 101 27.027 13.662 −15.063 1.00 24.51 C ATOM 2715 O TRP B 101 26.021 14.352 −15.030 1.00 28.72 O ATOM 2716 CB TRP B 101 25.908 11.380 −15.103 1.00 22.53 C ATOM 2717 CG TRP B 101 25.946 9.988 −15.686 1.00 25.58 C ATOM 2718 CD1 TRP B 101 26.400 8.852 −15.078 1.00 23.85 C ATOM 2719 CD2 TRP B 101 25.548 9.601 −17.005 1.00 24.91 C ATOM 2720 NE1 TRP B 101 26.299 7.776 −15.933 1.00 23.03 N ATOM 2721 CE2 TRP B 101 25.780 8.207 −17.122 1.00 23.56 C ATOM 2722 CE3 TRP B 101 25.006 10.289 −18.094 1.00 21.69 C ATOM 2723 CZ2 TRP B 101 25.480 7.491 −18.278 1.00 22.78 C ATOM 2724 CZ3 TRP B 101 24.714 9.577 −19.254 1.00 22.46 C ATOM 2725 CH2 TRP B 101 24.955 8.191 −19.335 1.00 26.38 C ATOM 2726 N GLY B 102 28.185 14.082 −14.566 1.00 30.91 N ATOM 2727 CA GLY B 102 28.325 15.438 −14.057 1.00 23.54 C ATOM 2728 C GLY B 102 28.298 15.578 −12.542 1.00 28.47 C ATOM 2729 O GLY B 102 27.739 14.745 −11.824 1.00 28.62 O ATOM 2730 N SER B 103 28.892 16.652 −12.043 1.00 22.82 N ATOM 2731 CA SER B 103 28.974 16.835 −10.599 1.00 25.49 C ATOM 2732 C SER B 103 27.596 16.851 −9.932 1.00 29.19 C ATOM 2733 O SER B 103 27.390 16.222 −8.899 1.00 29.30 O ATOM 2734 CB SER B 103 29.760 18.102 −10.250 1.00 25.41 C ATOM 2735 OG SER B 103 31.049 18.089 −10.853 1.00 40.23 O ATOM 2736 N PHE B 104 26.647 17.566 −10.516 1.00 24.16 N ATOM 2737 CA PHE B 104 25.350 17.671 −9.876 1.00 24.80 C ATOM 2738 C PHE B 104 24.639 16.332 −9.772 1.00 27.15 C ATOM 2739 O PHE B 104 24.100 16.003 −8.718 1.00 31.52 O ATOM 2740 CB PHE B 104 24.443 18.671 −10.583 1.00 30.47 C ATOM 2741 CG PHE B 104 23.043 18.665 −10.061 1.00 26.80 C ATOM 2742 CD1 PHE B 104 22.780 19.077 −8.764 1.00 26.69 C ATOM 2743 CD2 PHE B 104 21.994 18.221 −10.850 1.00 31.36 C ATOM 2744 CE1 PHE B 104 21.499 19.077 −8.271 1.00 21.80 C ATOM 2745 CE2 PHE B 104 20.702 18.211 −10.358 1.00 34.74 C ATOM 2746 CZ PHE B 104 20.456 18.641 −9.064 1.00 31.83 C ATOM 2747 N LEU B 105 24.621 15.568 −10.863 1.00 30.32 N ATOM 2748 CA LEU B 105 23.959 14.271 −10.840 1.00 25.78 C ATOM 2749 C LEU B 105 24.687 13.305 −9.920 1.00 25.33 C ATOM 2750 O LEU B 105 24.073 12.372 −9.395 1.00 23.85 O ATOM 2751 CB LEU B 105 23.819 13.671 −12.238 1.00 23.80 C ATOM 2752 CG LEU B 105 22.712 14.163 −13.172 1.00 28.25 C ATOM 2753 CD1 LEU B 105 22.323 13.042 −14.142 1.00 21.96 C ATOM 2754 CD2 LEU B 105 21.498 14.631 −12.395 1.00 29.70 C ATOM 2755 N CYS B 106 25.989 13.525 −9.727 1.00 22.99 N ATOM 2756 CA CYS B 106 26.765 12.688 −8.814 1.00 23.54 C ATOM 2757 C CYS B 106 26.190 12.797 −7.406 1.00 28.97 C ATOM 2758 O CYS B 106 25.909 11.779 −6.757 1.00 25.84 O ATOM 2759 CB CYS B 106 28.244 13.083 −8.802 1.00 24.33 C ATOM 2760 SG CYS B 106 29.251 12.142 −7.612 1.00 25.01 S ATOM 2761 N GLU B 107 26.013 14.038 −6.947 1.00 26.78 N ATOM 2762 CA GLU B 107 25.500 14.301 −5.614 1.00 23.89 C ATOM 2763 C GLU B 107 24.088 13.794 −5.483 1.00 23.83 C ATOM 2764 O GLU B 107 23.775 13.074 −4.546 1.00 17.95 O ATOM 2765 CB GLU B 107 25.571 15.785 −5.279 1.00 31.31 C ATOM 2766 CG GLU B 107 26.677 16.110 −4.283 1.00 53.35 C ATOM 2767 CD GLU B 107 26.605 17.535 −3.760 1.00 71.43 C ATOM 2768 OE1 GLU B 107 27.093 17.781 −2.622 1.00 59.99 O ATOM 2769 OE2 GLU B 107 26.057 18.396 −4.493 1.00 67.52 O ATOM 2770 N LEU B 108 23.250 14.155 −6.450 1.00 26.78 N ATOM 2771 CA LEU B 108 21.870 13.669 −6.505 1.00 28.67 C ATOM 2772 C LEU B 108 21.768 12.149 −6.419 1.00 25.50 C ATOM 2773 O LEU B 108 20.956 11.624 −5.659 1.00 29.97 O ATOM 2774 CB LEU B 108 21.166 14.153 −7.771 1.00 23.10 C ATOM 2775 CG LEU B 108 19.660 13.978 −7.655 1.00 23.03 C ATOM 2776 CD1 LEU B 108 19.157 14.893 −6.542 1.00 23.50 C ATOM 2777 CD2 LEU B 108 18.967 14.276 −8.996 1.00 21.21 C ATOM 2778 N TRP B 109 22.585 11.456 −7.211 1.00 25.65 N ATOM 2779 CA TRP B 109 22.618 9.999 −7.223 1.00 22.11 C ATOM 2780 C TRP B 109 22.949 9.473 −5.831 1.00 26.27 C ATOM 2781 O TRP B 109 22.277 8.576 −5.328 1.00 28.84 O ATOM 2782 CB TRP B 109 23.642 9.496 −8.259 1.00 20.36 C ATOM 2783 CG TRP B 109 23.961 8.020 −8.161 1.00 21.75 C ATOM 2784 CD1 TRP B 109 23.114 6.977 −8.415 1.00 23.62 C ATOM 2785 CD2 TRP B 109 25.212 7.433 −7.779 1.00 17.80 C ATOM 2786 NE1 TRP B 109 23.756 5.782 −8.210 1.00 19.75 N ATOM 2787 CE2 TRP B 109 25.044 6.031 −7.817 1.00 20.67 C ATOM 2788 CE3 TRP B 109 26.454 7.954 −7.410 1.00 24.00 C ATOM 2789 CZ2 TRP B 109 26.078 5.141 −7.498 1.00 19.81 C ATOM 2790 CZ3 TRP B 109 27.480 7.071 −7.094 1.00 27.21 C ATOM 2791 CH2 TRP B 109 27.283 5.681 −7.140 1.00 23.73 C ATOM 2792 N THR B 110 23.986 10.042 −5.222 1.00 24.38 N ATOM 2793 CA THR B 110 24.449 9.634 −3.904 1.00 24.83 C ATOM 2794 C THR B 110 23.351 9.824 −2.853 1.00 23.81 C ATOM 2795 O THR B 110 23.055 8.905 −2.109 1.00 27.17 O ATOM 2796 CB THR B 110 25.739 10.410 −3.509 1.00 25.69 C ATOM 2797 OG1 THR B 110 26.793 10.058 −4.412 1.00 27.99 O ATOM 2798 CG2 THR B 110 26.180 10.093 −2.075 1.00 14.32 C ATOM 2799 N SER B 111 22.758 11.014 −2.799 1.00 23.96 N ATOM 2800 CA SER B 111 21.563 11.270 −1.994 1.00 24.92 C ATOM 2801 C SER B 111 20.506 10.156 −2.099 1.00 32.13 C ATOM 2802 O SER B 111 19.967 9.699 −1.075 1.00 21.22 O ATOM 2803 CB SER B 111 20.913 12.586 −2.419 1.00 25.11 C ATOM 2804 OG SER B 111 21.713 13.694 −2.058 1.00 35.53 O ATOM 2805 N LEU B 112 20.210 9.737 −3.334 1.00 20.40 N ATOM 2806 CA LEU B 112 19.181 8.732 −3.604 1.00 22.72 C ATOM 2807 C LEU B 112 19.499 7.368 −3.055 1.00 24.74 C ATOM 2808 O LEU B 112 18.628 6.656 −2.554 1.00 27.64 O ATOM 2809 CB LEU B 112 18.983 8.572 −5.096 1.00 21.13 C ATOM 2810 CG LEU B 112 17.857 9.423 −5.637 1.00 35.52 C ATOM 2811 CD1 LEU B 112 17.523 8.949 −7.045 1.00 28.77 C ATOM 2812 CD2 LEU B 112 16.651 9.337 −4.685 1.00 23.06 C ATOM 2813 N ASP B 113 20.755 7.001 −3.201 1.00 19.58 N ATOM 2814 CA ASP B 113 21.250 5.717 −2.774 1.00 26.51 C ATOM 2815 C ASP B 113 21.042 5.564 −1.269 1.00 26.23 C ATOM 2816 O ASP B 113 20.491 4.569 −0.800 1.00 27.54 O ATOM 2817 CB ASP B 113 22.735 5.670 −3.128 1.00 30.13 C ATOM 2818 CG ASP B 113 23.356 4.330 −2.892 1.00 28.63 C ATOM 2819 OD1 ASP B 113 22.804 3.531 −2.105 1.00 31.60 O ATOM 2820 OD2 ASP B 113 24.416 4.092 −3.493 1.00 28.09 O ATOM 2821 N VAL B 114 21.479 6.581 −0.538 1.00 21.39 N ATOM 2822 CA VAL B 114 21.434 6.623 0.918 1.00 24.98 C ATOM 2823 C VAL B 114 20.007 6.675 1.462 1.00 24.83 C ATOM 2824 O VAL B 114 19.663 5.980 2.430 1.00 21.53 O ATOM 2825 CB VAL B 114 22.258 7.832 1.434 1.00 28.12 C ATOM 2826 CG1 VAL B 114 22.135 7.984 2.922 1.00 23.27 C ATOM 2827 CG2 VAL B 114 23.720 7.646 1.069 1.00 28.64 C ATOM 2828 N LEU B 115 19.181 7.503 0.834 1.00 26.86 N ATOM 2829 CA LEU B 115 17.753 7.572 1.151 1.00 20.55 C ATOM 2830 C LEU B 115 17.083 6.205 1.074 1.00 23.52 C ATOM 2831 O LEU B 115 16.332 5.831 1.977 1.00 24.11 O ATOM 2832 CB LEU B 115 17.042 8.539 0.206 1.00 19.11 C ATOM 2833 CG LEU B 115 15.553 8.698 0.472 1.00 22.12 C ATOM 2834 CD1 LEU B 115 15.321 9.013 1.935 1.00 21.95 C ATOM 2835 CD2 LEU B 115 15.012 9.793 −0.405 1.00 21.91 C ATOM 2836 N CYS B 116 17.360 5.459 0.002 1.00 22.70 N ATOM 2837 CA CYS B 116 16.734 4.147 −0.183 1.00 31.84 C ATOM 2838 C CYS B 116 17.123 3.104 0.878 1.00 32.18 C ATOM 2839 O CYS B 116 16.287 2.302 1.287 1.00 32.32 O ATOM 2840 CB CYS B 116 16.966 3.600 −1.596 1.00 20.17 C ATOM 2841 SG CYS B 116 16.019 4.461 −2.846 1.00 40.86 S ATOM 2842 N VAL B 117 18.374 3.116 1.326 1.00 22.95 N ATOM 2843 CA VAL B 117 18.794 2.187 2.372 1.00 31.86 C ATOM 2844 C VAL B 117 18.292 2.616 3.762 1.00 35.14 C ATOM 2845 O VAL B 117 17.927 1.769 4.584 1.00 23.25 O ATOM 2846 CB VAL B 117 20.329 1.985 2.404 1.00 27.89 C ATOM 2847 CG1 VAL B 117 20.681 0.799 3.287 1.00 29.36 C ATOM 2848 CG2 VAL B 117 20.856 1.765 1.016 1.00 23.68 C ATOM 2849 N THR B 118 18.274 3.923 4.024 1.00 29.96 N ATOM 2850 CA THR B 118 17.734 4.412 5.285 1.00 30.83 C ATOM 2851 C THR B 118 16.255 4.048 5.408 1.00 29.14 C ATOM 2852 O THR B 118 15.827 3.541 6.444 1.00 22.53 O ATOM 2853 CB THR B 118 17.888 5.943 5.437 1.00 33.94 C ATOM 2854 OG1 THR B 118 19.275 6.298 5.415 1.00 28.33 O ATOM 2855 CG2 THR B 118 17.262 6.423 6.745 1.00 22.28 C ATOM 2856 N ALA B 119 15.487 4.300 4.345 1.00 23.77 N ATOM 2857 CA ALA B 119 14.044 4.043 4.366 1.00 23.58 C ATOM 2858 C ALA B 119 13.688 2.549 4.490 1.00 23.51 C ATOM 2859 O ALA B 119 12.684 2.195 5.091 1.00 27.98 O ATOM 2860 CB ALA B 119 13.354 4.686 3.168 1.00 21.64 C ATOM 2861 N SER B 120 14.522 1.676 3.944 1.00 27.68 N ATOM 2862 CA SER B 120 14.299 0.236 4.063 1.00 29.85 C ATOM 2863 C SER B 120 14.371 −0.213 5.515 1.00 27.06 C ATOM 2864 O SER B 120 13.384 −0.693 6.063 1.00 30.48 O ATOM 2865 CB SER B 120 15.312 −0.569 3.237 1.00 24.87 C ATOM 2866 OG SER B 120 15.134 −0.371 1.853 1.00 35.56 O ATOM 2867 N ILE B 121 15.548 −0.068 6.121 1.00 22.70 N ATOM 2868 CA ILE B 121 15.761 −0.487 7.499 1.00 26.14 C ATOM 2869 C ILE B 121 14.727 0.192 8.410 1.00 27.72 C ATOM 2870 O ILE B 121 14.164 −0.438 9.298 1.00 27.02 O ATOM 2871 CB ILE B 121 17.222 −0.224 7.978 1.00 21.40 C ATOM 2872 CG1 ILE B 121 17.555 −1.041 9.228 1.00 23.57 C ATOM 2873 CG2 ILE B 121 17.447 1.247 8.259 1.00 20.63 C ATOM 2874 CD1 ILE B 121 17.120 −2.472 9.164 1.00 30.47 C ATOM 2875 N GLU B 122 14.452 1.468 8.163 1.00 32.55 N ATOM 2876 CA GLU B 122 13.445 2.173 8.949 1.00 29.38 C ATOM 2877 C GLU B 122 12.087 1.514 8.816 1.00 29.68 C ATOM 2878 O GLU B 122 11.362 1.392 9.800 1.00 28.19 O ATOM 2879 CB GLU B 122 13.348 3.647 8.552 1.00 27.52 C ATOM 2880 CG GLU B 122 14.275 4.565 9.335 1.00 28.18 C ATOM 2881 CD GLU B 122 13.991 6.044 9.071 1.00 42.72 C ATOM 2882 OE1 GLU B 122 12.911 6.362 8.528 1.00 39.95 O ATOM 2883 OE2 GLU B 122 14.845 6.895 9.411 1.00 45.99 O ATOM 2884 N THR B 123 11.741 1.095 7.599 1.00 32.57 N ATOM 2885 CA THR B 123 10.471 0.414 7.361 1.00 28.73 C ATOM 2886 C THR B 123 10.455 −0.975 7.999 1.00 32.15 C ATOM 2887 O THR B 123 9.474 −1.368 8.614 1.00 31.18 O ATOM 2888 CB THR B 123 10.154 0.304 5.866 1.00 28.74 C ATOM 2889 OG1 THR B 123 9.810 1.596 5.364 1.00 32.13 O ATOM 2890 CG2 THR B 123 8.988 −0.638 5.632 1.00 29.92 C ATOM 2891 N LEU B 124 11.544 −1.718 7.858 1.00 30.78 N ATOM 2892 CA LEU B 124 11.631 −3.025 8.488 1.00 30.84 C ATOM 2893 C LEU B 124 11.421 −2.893 9.989 1.00 33.17 C ATOM 2894 O LEU B 124 10.918 −3.797 10.651 1.00 39.00 O ATOM 2895 CB LEU B 124 12.983 −3.668 8.183 1.00 33.47 C ATOM 2896 CG LEU B 124 13.043 −4.233 6.759 1.00 28.66 C ATOM 2897 CD1 LEU B 124 14.462 −4.628 6.351 1.00 29.17 C ATOM 2898 CD2 LEU B 124 12.105 −5.410 6.670 1.00 32.69 C ATOM 2899 N CYS B 125 11.806 −1.749 10.526 1.00 35.71 N ATOM 2900 CA CYS B 125 11.635 −1.491 11.943 1.00 39.83 C ATOM 2901 C CYS B 125 10.146 −1.432 12.249 1.00 36.88 C ATOM 2902 O CYS B 125 9.635 −2.169 13.086 1.00 36.27 O ATOM 2903 CB CYS B 125 12.286 −0.162 12.303 1.00 36.68 C ATOM 2904 SG CYS B 125 13.359 −0.278 13.695 1.00 49.77 S ATOM 2905 N VAL B 126 9.455 −0.546 11.546 1.00 31.52 N ATOM 2906 CA VAL B 126 8.025 −0.407 11.705 1.00 28.31 C ATOM 2907 C VAL B 126 7.307 −1.753 11.580 1.00 32.71 C ATOM 2908 O VAL B 126 6.496 −2.086 12.431 1.00 43.13 O ATOM 2909 CB VAL B 126 7.464 0.644 10.741 1.00 29.20 C ATOM 2910 CG1 VAL B 126 5.944 0.555 10.653 1.00 32.82 C ATOM 2911 CG2 VAL B 126 7.905 2.024 11.184 1.00 22.76 C ATOM 2912 N ILE B 127 7.617 −2.531 10.547 1.00 30.89 N ATOM 2913 CA ILE B 127 7.056 −3.877 10.391 1.00 34.33 C ATOM 2914 C ILE B 127 7.192 −4.711 11.672 1.00 41.02 C ATOM 2915 O ILE B 127 6.238 −5.365 12.099 1.00 43.20 O ATOM 2916 CB ILE B 127 7.737 −4.664 9.231 1.00 49.96 C ATOM 2917 CG1 ILE B 127 7.315 −4.127 7.861 1.00 35.86 C ATOM 2918 CG2 ILE B 127 7.434 −6.174 9.316 1.00 35.81 C ATOM 2919 CD1 ILE B 127 8.134 −4.729 6.737 1.00 36.93 C ATOM 2920 N ALA B 128 8.370 −4.697 12.287 1.00 29.58 N ATOM 2921 CA ALA B 128 8.588 −5.494 13.491 1.00 31.62 C ATOM 2922 C ALA B 128 7.773 −4.984 14.675 1.00 39.85 C ATOM 2923 O ALA B 128 7.077 −5.754 15.331 1.00 49.30 O ATOM 2924 CB ALA B 128 10.067 −5.546 13.843 1.00 37.51 C ATOM 2925 N ILE B 129 7.866 −3.685 14.942 1.00 35.48 N ATOM 2926 CA ILE B 129 7.127 −3.052 16.026 1.00 35.81 C ATOM 2927 C ILE B 129 5.615 −3.220 15.875 1.00 38.43 C ATOM 2928 O ILE B 129 4.896 −3.353 16.859 1.00 39.36 O ATOM 2929 CB ILE B 129 7.440 −1.547 16.100 1.00 42.07 C ATOM 2930 CG1 ILE B 129 8.877 −1.327 16.574 1.00 36.46 C ATOM 2931 CG2 ILE B 129 6.432 −0.823 17.008 1.00 29.72 C ATOM 2932 CD1 ILE B 129 9.311 0.115 16.497 1.00 29.25 C ATOM 2933 N ASP B 130 5.143 −3.191 14.635 1.00 38.72 N ATOM 2934 CA ASP B 130 3.730 −3.367 14.319 1.00 37.47 C ATOM 2935 C ASP B 130 3.277 −4.763 14.711 1.00 39.01 C ATOM 2936 O ASP B 130 2.281 −4.927 15.403 1.00 36.78 O ATOM 2937 CB ASP B 130 3.507 −3.124 12.819 1.00 38.15 C ATOM 2938 CG ASP B 130 2.348 −3.933 12.245 1.00 53.55 C ATOM 2939 OD1 ASP B 130 1.202 −3.716 12.688 1.00 64.40 O ATOM 2940 OD2 ASP B 130 2.576 −4.768 11.331 1.00 54.68 O ATOM 2941 N ARG B 131 4.022 −5.764 14.255 1.00 41.77 N ATOM 2942 CA ARG B 131 3.760 −7.151 14.602 1.00 45.38 C ATOM 2943 C ARG B 131 3.791 −7.350 16.113 1.00 41.25 C ATOM 2944 O ARG B 131 2.918 −8.001 16.677 1.00 36.53 O ATOM 2945 CB ARG B 131 4.791 −8.067 13.933 1.00 42.90 C ATOM 2946 CG ARG B 131 4.585 −8.251 12.438 1.00 41.24 C ATOM 2947 CD ARG B 131 3.193 −8.765 12.122 1.00 40.05 C ATOM 2948 NE ARG B 131 2.207 −7.692 12.047 1.00 51.13 N ATOM 2949 CZ ARG B 131 0.895 −7.889 11.964 1.00 57.15 C ATOM 2950 NH1 ARG B 131 0.410 −9.128 11.954 1.00 59.37 N ATOM 2951 NH2 ARG B 131 0.067 −6.852 11.899 1.00 42.60 N ATOM 2952 N TYR B 132 4.806 −6.793 16.764 1.00 35.87 N ATOM 2953 CA TYR B 132 4.923 −6.935 18.204 1.00 47.68 C ATOM 2954 C TYR B 132 3.740 −6.333 18.970 1.00 51.85 C ATOM 2955 O TYR B 132 3.397 −6.803 20.053 1.00 53.14 O ATOM 2956 CB TYR B 132 6.229 −6.337 18.720 1.00 48.84 C ATOM 2957 CG TYR B 132 6.307 −6.352 20.224 1.00 41.78 C ATOM 2958 CD1 TYR B 132 6.784 −7.463 20.901 1.00 49.77 C ATOM 2959 CD2 TYR B 132 5.878 −5.263 20.965 1.00 50.94 C ATOM 2960 CE1 TYR B 132 6.843 −7.484 22.274 1.00 53.70 C ATOM 2961 CE2 TYR B 132 5.938 −5.271 22.332 1.00 57.21 C ATOM 2962 CZ TYR B 132 6.418 −6.385 22.982 1.00 58.95 C ATOM 2963 OH TYR B 132 6.467 −6.393 24.352 1.00 72.24 O ATOM 2964 N LEU B 133 3.130 −5.288 18.423 1.00 42.80 N ATOM 2965 CA LEU B 133 1.929 −4.725 19.020 1.00 39.15 C ATOM 2966 C LEU B 133 0.697 −5.587 18.722 1.00 44.17 C ATOM 2967 O LEU B 133 −0.135 −5.819 19.595 1.00 47.92 O ATOM 2968 CB LEU B 133 1.698 −3.292 18.541 1.00 32.41 C ATOM 2969 CG LEU B 133 2.715 −2.218 18.928 1.00 37.90 C ATOM 2970 CD1 LEU B 133 2.348 −0.900 18.249 1.00 30.23 C ATOM 2971 CD2 LEU B 133 2.825 −2.032 20.443 1.00 32.12 C ATOM 2972 N ALA B 134 0.578 −6.059 17.488 1.00 46.03 N ATOM 2973 CA ALA B 134 −0.567 −6.869 17.107 1.00 43.43 C ATOM 2974 C ALA B 134 −0.584 −8.115 17.963 1.00 42.33 C ATOM 2975 O ALA B 134 −1.630 −8.554 18.420 1.00 51.73 O ATOM 2976 CB ALA B 134 −0.513 −7.230 15.628 1.00 26.95 C ATOM 2977 N ILE B 135 0.594 −8.666 18.207 1.00 52.56 N ATOM 2978 CA ILE B 135 0.699 −9.939 18.899 1.00 57.12 C ATOM 2979 C ILE B 135 0.463 −9.812 20.410 1.00 53.25 C ATOM 2980 O ILE B 135 −0.121 −10.708 21.016 1.00 58.54 O ATOM 2981 CB ILE B 135 2.055 −10.614 18.619 1.00 59.12 C ATOM 2982 CG1 ILE B 135 1.856 −12.039 18.118 1.00 50.85 C ATOM 2983 CG2 ILE B 135 2.945 −10.578 19.856 1.00 66.10 C ATOM 2984 CD1 ILE B 135 3.163 −12.765 17.882 1.00 65.69 C ATOM 2985 N THR B 136 0.900 −8.707 21.015 1.00 51.61 N ATOM 2986 CA THR B 136 0.699 −8.508 22.459 1.00 47.78 C ATOM 2987 C THR B 136 −0.581 −7.740 22.824 1.00 54.84 C ATOM 2988 O THR B 136 −1.180 −8.015 23.858 1.00 52.93 O ATOM 2989 CB THR B 136 1.896 −7.802 23.159 1.00 52.23 C ATOM 2990 OG1 THR B 136 1.894 −6.400 22.842 1.00 46.45 O ATOM 2991 CG2 THR B 136 3.233 −8.448 22.779 1.00 46.53 C ATOM 2992 N SER B 137 −0.997 −6.784 21.992 1.00 57.43 N ATOM 2993 CA SER B 137 −2.157 −5.942 22.319 1.00 47.89 C ATOM 2994 C SER B 137 −3.302 −5.990 21.310 1.00 48.29 C ATOM 2995 O SER B 137 −3.835 −4.945 20.933 1.00 49.37 O ATOM 2996 CB SER B 137 −1.726 −4.484 22.483 1.00 44.38 C ATOM 2997 OG SER B 137 −0.867 −4.324 23.591 1.00 60.02 O ATOM 2998 N PRO B 138 −3.708 −7.197 20.892 1.00 52.06 N ATOM 2999 CA PRO B 138 −4.699 −7.358 19.818 1.00 57.37 C ATOM 3000 C PRO B 138 −5.893 −6.401 19.873 1.00 59.27 C ATOM 3001 O PRO B 138 −6.288 −5.894 18.823 1.00 65.54 O ATOM 3002 CB PRO B 138 −5.163 −8.812 19.990 1.00 40.41 C ATOM 3003 CG PRO B 138 −4.621 −9.230 21.335 1.00 57.14 C ATOM 3004 CD PRO B 138 −3.337 −8.500 21.450 1.00 40.00 C ATOM 3005 N PHE B 139 −6.459 −6.161 21.053 1.00 61.30 N ATOM 3006 CA PHE B 139 −7.629 −5.287 21.158 1.00 62.66 C ATOM 3007 C PHE B 139 −7.265 −3.812 21.004 1.00 57.87 C ATOM 3008 O PHE B 139 −7.909 −3.086 20.248 1.00 67.75 O ATOM 3009 CB PHE B 139 −8.394 −5.514 22.469 1.00 83.75 C ATOM 3010 CG PHE B 139 −9.665 −4.707 22.578 1.00 92.58 C ATOM 3011 CD1 PHE B 139 −10.861 −5.200 22.078 1.00 91.86 C ATOM 3012 CD2 PHE B 139 −9.660 −3.449 23.168 1.00 85.95 C ATOM 3013 CE1 PHE B 139 −12.028 −4.455 22.167 1.00 86.07 C ATOM 3014 CE2 PHE B 139 −10.823 −2.701 23.258 1.00 81.86 C ATOM 3015 CZ PHE B 139 −12.006 −3.205 22.757 1.00 82.49 C ATOM 3016 N ARG B 140 −6.239 −3.366 21.715 1.00 52.27 N ATOM 3017 CA ARG B 140 −5.794 −1.983 21.589 1.00 57.00 C ATOM 3018 C ARG B 140 −5.163 −1.719 20.228 1.00 58.08 C ATOM 3019 O ARG B 140 −4.957 −0.572 19.843 1.00 67.10 O ATOM 3020 CB ARG B 140 −4.826 −1.606 22.708 1.00 55.01 C ATOM 3021 CG ARG B 140 −5.506 −1.336 24.037 1.00 58.27 C ATOM 3022 CD ARG B 140 −4.518 −0.792 25.051 1.00 73.82 C ATOM 3023 NE ARG B 140 −5.188 −0.319 26.259 1.00 88.96 N ATOM 3024 CZ ARG B 140 −4.581 0.361 27.226 1.00 91.96 C ATOM 3025 NH1 ARG B 140 −3.289 0.646 27.121 1.00 91.58 N ATOM 3026 NH2 ARG B 140 −5.261 0.760 28.293 1.00 83.70 N ATOM 3027 N TYR B 141 −4.870 −2.784 19.494 1.00 55.37 N ATOM 3028 CA TYR B 141 −4.294 −2.655 18.160 1.00 50.90 C ATOM 3029 C TYR B 141 −5.333 −2.402 17.060 1.00 61.21 C ATOM 3030 O TYR B 141 −5.179 −1.470 16.272 1.00 60.06 O ATOM 3031 CB TYR B 141 −3.452 −3.884 17.826 1.00 53.15 C ATOM 3032 CG TYR B 141 −2.849 −3.861 16.443 1.00 52.99 C ATOM 3033 CD1 TYR B 141 −1.631 −3.239 16.200 1.00 57.12 C ATOM 3034 CD2 TYR B 141 −3.502 −4.463 15.379 1.00 60.99 C ATOM 3035 CE1 TYR B 141 −1.085 −3.220 14.926 1.00 59.63 C ATOM 3036 CE2 TYR B 141 −2.969 −4.449 14.113 1.00 58.95 C ATOM 3037 CZ TYR B 141 −1.762 −3.831 13.885 1.00 57.45 C ATOM 3038 OH TYR B 141 −1.245 −3.831 12.608 1.00 57.25 O ATOM 3039 N GLN B 142 −6.379 −3.230 17.009 1.00 64.26 N ATOM 3040 CA GLN B 142 −7.442 −3.109 16.002 1.00 70.94 C ATOM 3041 C GLN B 142 −8.073 −1.716 15.917 1.00 73.96 C ATOM 3042 O GLN B 142 −8.322 −1.197 14.822 1.00 72.85 O ATOM 3043 CB GLN B 142 −8.560 −4.107 16.285 1.00 87.97 C ATOM 3044 CG GLN B 142 −8.303 −5.527 15.838 1.00 97.92 C ATOM 3045 CD GLN B 142 −9.432 −6.457 16.254 1.00 121.46 C ATOM 3046 OE1 GLN B 142 −10.584 −6.030 16.412 1.00 102.41 O ATOM 3047 NE2 GLN B 142 −9.106 −7.732 16.445 1.00 119.33 N ATOM 3048 N SER B 143 −8.353 −1.128 17.076 1.00 67.38 N ATOM 3049 CA SER B 143 −9.030 0.164 17.131 1.00 68.27 C ATOM 3050 C SER B 143 −8.125 1.315 16.702 1.00 71.56 C ATOM 3051 O SER B 143 −8.559 2.212 15.979 1.00 75.84 O ATOM 3052 CB SER B 143 −9.631 0.417 18.526 1.00 78.89 C ATOM 3053 OG SER B 143 −8.974 −0.337 19.535 1.00 70.07 O ATOM 3054 N LEU B 144 −6.866 1.279 17.132 1.00 62.02 N ATOM 3055 CA LEU B 144 −5.927 2.344 16.802 1.00 60.71 C ATOM 3056 C LEU B 144 −5.374 2.267 15.373 1.00 61.44 C ATOM 3057 O LEU B 144 −5.156 3.293 14.729 1.00 60.22 O ATOM 3058 CB LEU B 144 −4.796 2.398 17.831 1.00 56.74 C ATOM 3059 CG LEU B 144 −5.348 2.731 19.215 1.00 66.86 C ATOM 3060 CD1 LEU B 144 −4.256 3.170 20.178 1.00 46.16 C ATOM 3061 CD2 LEU B 144 −6.413 3.808 19.076 1.00 57.79 C ATOM 3062 N MET B 145 −5.159 1.060 14.868 1.00 52.98 N ATOM 3063 CA MET B 145 −4.512 0.908 13.568 1.00 60.61 C ATOM 3064 C MET B 145 −5.464 0.693 12.388 1.00 53.88 C ATOM 3065 O MET B 145 −5.989 −0.396 12.198 1.00 54.51 O ATOM 3066 CB MET B 145 −3.470 −0.214 13.624 1.00 57.45 C ATOM 3067 CG MET B 145 −2.083 0.241 14.073 1.00 69.20 C ATOM 3068 SD MET B 145 −0.952 0.582 12.698 1.00 82.47 S ATOM 3069 CE MET B 145 −1.624 2.108 12.041 1.00 55.15 C ATOM 3070 N THR B 146 −5.673 1.744 11.601 1.00 43.69 N ATOM 3071 CA THR B 146 −6.393 1.643 10.339 1.00 39.91 C ATOM 3072 C THR B 146 −5.399 1.713 9.175 1.00 51.53 C ATOM 3073 O THR B 146 −4.188 1.705 9.396 1.00 56.89 O ATOM 3074 CB THR B 146 −7.464 2.751 10.198 1.00 55.94 C ATOM 3075 OG1 THR B 146 −6.845 4.045 10.230 1.00 52.14 O ATOM 3076 CG2 THR B 146 −8.494 2.646 11.322 1.00 51.55 C ATOM 3077 N ARG B 147 −5.894 1.775 7.941 1.00 53.99 N ATOM 3078 CA ARG B 147 −5.010 1.844 6.775 1.00 36.41 C ATOM 3079 C ARG B 147 −4.578 3.273 6.475 1.00 44.20 C ATOM 3080 O ARG B 147 −3.489 3.500 5.952 1.00 49.25 O ATOM 3081 CB ARG B 147 −5.680 1.256 5.532 1.00 54.91 C ATOM 3082 CG ARG B 147 −5.843 −0.242 5.553 1.00 68.69 C ATOM 3083 CD ARG B 147 −6.363 −0.734 4.221 1.00 73.99 C ATOM 3084 NE ARG B 147 −6.896 −2.086 4.327 1.00 83.99 N ATOM 3085 CZ ARG B 147 −7.809 −2.583 3.503 1.00 88.03 C ATOM 3086 NH1 ARG B 147 −8.287 −1.829 2.520 1.00 91.81 N ATOM 3087 NH2 ARG B 147 −8.250 −3.824 3.667 1.00 82.20 N ATOM 3088 N ALA B 148 −5.431 4.240 6.792 1.00 47.27 N ATOM 3089 CA ALA B 148 −5.082 5.631 6.558 1.00 46.62 C ATOM 3090 C ALA B 148 −3.859 5.994 7.387 1.00 40.08 C ATOM 3091 O ALA B 148 −3.060 6.847 6.994 1.00 43.11 O ATOM 3092 CB ALA B 148 −6.245 6.534 6.886 1.00 37.66 C ATOM 3093 N ARG B 149 −3.710 5.319 8.521 1.00 31.19 N ATOM 3094 CA ARG B 149 −2.613 5.589 9.436 1.00 47.60 C ATOM 3095 C ARG B 149 −1.299 4.927 9.047 1.00 43.94 C ATOM 3096 O ARG B 149 −0.229 5.515 9.218 1.00 34.83 O ATOM 3097 CB ARG B 149 −3.009 5.237 10.869 1.00 46.20 C ATOM 3098 CG ARG B 149 −3.860 6.319 11.489 1.00 49.51 C ATOM 3099 CD ARG B 149 −4.276 6.006 12.901 1.00 53.03 C ATOM 3100 NE ARG B 149 −5.336 6.919 13.295 1.00 57.25 N ATOM 3101 CZ ARG B 149 −6.246 6.650 14.217 1.00 59.07 C ATOM 3102 NH1 ARG B 149 −6.221 5.485 14.847 1.00 54.96 N ATOM 3103 NH2 ARG B 149 −7.181 7.546 14.502 1.00 71.12 N ATOM 3104 N ALA B 150 −1.382 3.709 8.529 1.00 36.22 N ATOM 3105 CA ALA B 150 −0.204 3.054 7.988 1.00 38.88 C ATOM 3106 C ALA B 150 0.393 3.904 6.860 1.00 37.17 C ATOM 3107 O ALA B 150 1.612 4.081 6.785 1.00 33.88 O ATOM 3108 CB ALA B 150 −0.544 1.656 7.497 1.00 41.50 C ATOM 3109 N LYS B 151 −0.460 4.437 5.990 1.00 30.74 N ATOM 3110 CA LYS B 151 0.002 5.375 4.976 1.00 31.80 C ATOM 3111 C LYS B 151 0.681 6.585 5.631 1.00 41.80 C ATOM 3112 O LYS B 151 1.792 6.983 5.239 1.00 36.84 O ATOM 3113 CB LYS B 151 −1.142 5.842 4.086 1.00 25.15 C ATOM 3114 CG LYS B 151 −1.673 4.806 3.112 1.00 40.94 C ATOM 3115 CD LYS B 151 −2.760 5.433 2.236 1.00 58.78 C ATOM 3116 CE LYS B 151 −3.876 4.450 1.894 1.00 66.59 C ATOM 3117 NZ LYS B 151 −5.175 5.168 1.690 1.00 60.94 N ATOM 3118 N VAL B 152 0.019 7.166 6.631 1.00 39.15 N ATOM 3119 CA VAL B 152 0.611 8.276 7.373 1.00 36.37 C ATOM 3120 C VAL B 152 1.944 7.860 8.003 1.00 31.40 C ATOM 3121 O VAL B 152 2.902 8.624 7.988 1.00 27.52 O ATOM 3122 CB VAL B 152 −0.348 8.850 8.430 1.00 32.18 C ATOM 3123 CG1 VAL B 152 0.413 9.715 9.418 1.00 39.20 C ATOM 3124 CG2 VAL B 152 −1.414 9.658 7.759 1.00 30.88 C ATOM 3125 N ILE B 153 2.008 6.644 8.535 1.00 28.94 N ATOM 3126 CA ILE B 153 3.262 6.131 9.071 1.00 30.79 C ATOM 3127 C ILE B 153 4.334 5.984 7.987 1.00 28.84 C ATOM 3128 O ILE B 153 5.462 6.444 8.162 1.00 21.84 O ATOM 3129 CB ILE B 153 3.074 4.788 9.780 1.00 28.22 C ATOM 3130 CG1 ILE B 153 2.172 4.971 10.995 1.00 35.39 C ATOM 3131 CG2 ILE B 153 4.431 4.207 10.196 1.00 24.84 C ATOM 3132 CD1 ILE B 153 1.869 3.692 11.736 1.00 30.64 C ATOM 3133 N ILE B 154 3.982 5.340 6.875 1.00 26.13 N ATOM 3134 CA ILE B 154 4.917 5.174 5.768 1.00 28.18 C ATOM 3135 C ILE B 154 5.484 6.525 5.318 1.00 33.03 C ATOM 3136 O ILE B 154 6.706 6.694 5.191 1.00 24.88 O ATOM 3137 CB ILE B 154 4.267 4.459 4.579 1.00 27.18 C ATOM 3138 CG1 ILE B 154 4.206 2.951 4.841 1.00 33.18 C ATOM 3139 CG2 ILE B 154 5.053 4.740 3.307 1.00 24.58 C ATOM 3140 CD1 ILE B 154 3.066 2.240 4.117 1.00 28.80 C ATOM 3141 N CYS B 155 4.592 7.488 5.090 1.00 27.81 N ATOM 3142 CA CYS B 155 5.010 8.841 4.743 1.00 24.89 C ATOM 3143 C CYS B 155 5.993 9.461 5.746 1.00 31.35 C ATOM 3144 O CYS B 155 6.936 10.150 5.364 1.00 28.69 O ATOM 3145 CB CYS B 155 3.792 9.739 4.594 1.00 20.06 C ATOM 3146 SG CYS B 155 2.939 9.455 3.069 1.00 41.60 S ATOM 3147 N THR B 156 5.762 9.220 7.031 1.00 29.60 N ATOM 3148 CA THR B 156 6.619 9.774 8.065 1.00 30.92 C ATOM 3149 C THR B 156 8.015 9.133 8.037 1.00 25.63 C ATOM 3150 O THR B 156 9.024 9.828 8.173 1.00 23.09 O ATOM 3151 CB THR B 156 5.942 9.701 9.453 1.00 21.61 C ATOM 3152 OG1 THR B 156 4.682 10.364 9.374 1.00 39.16 O ATOM 3153 CG2 THR B 156 6.766 10.410 10.503 1.00 21.31 C ATOM 3154 N VAL B 157 8.075 7.822 7.830 1.00 21.35 N ATOM 3155 CA VAL B 157 9.361 7.163 7.616 1.00 30.10 C ATOM 3156 C VAL B 157 10.140 7.752 6.410 1.00 28.51 C ATOM 3157 O VAL B 157 11.345 7.984 6.495 1.00 26.93 O ATOM 3158 CB VAL B 157 9.211 5.622 7.490 1.00 23.99 C ATOM 3159 CG1 VAL B 157 10.514 4.982 7.015 1.00 21.87 C ATOM 3160 CG2 VAL B 157 8.780 5.036 8.805 1.00 19.41 C ATOM 3161 N TRP B 158 9.464 8.014 5.300 1.00 19.52 N ATOM 3162 CA TRP B 158 10.166 8.599 4.168 1.00 21.62 C ATOM 3163 C TRP B 158 10.610 10.043 4.446 1.00 21.29 C ATOM 3164 O TRP B 158 11.593 10.502 3.881 1.00 20.92 O ATOM 3165 CB TRP B 158 9.348 8.488 2.860 1.00 25.60 C ATOM 3166 CG TRP B 158 9.391 7.111 2.223 1.00 21.80 C ATOM 3167 CD1 TRP B 158 8.512 6.093 2.425 1.00 20.83 C ATOM 3168 CD2 TRP B 158 10.375 6.610 1.306 1.00 28.29 C ATOM 3169 NE1 TRP B 158 8.880 4.987 1.699 1.00 22.95 N ATOM 3170 CE2 TRP B 158 10.020 5.273 1.004 1.00 25.48 C ATOM 3171 CE3 TRP B 158 11.527 7.152 0.723 1.00 29.57 C ATOM 3172 CZ2 TRP B 158 10.758 4.480 0.133 1.00 24.46 C ATOM 3173 CZ3 TRP B 158 12.268 6.356 −0.142 1.00 33.93 C ATOM 3174 CH2 TRP B 158 11.875 5.035 −0.430 1.00 34.66 C ATOM 3175 N ALA B 159 9.905 10.755 5.322 1.00 20.11 N ATOM 3176 CA ALA B 159 10.306 12.118 5.678 1.00 19.20 C ATOM 3177 C ALA B 159 11.503 12.082 6.600 1.00 24.32 C ATOM 3178 O ALA B 159 12.500 12.776 6.375 1.00 24.74 O ATOM 3179 CB ALA B 159 9.172 12.877 6.341 1.00 18.08 C ATOM 3180 N ILE B 160 11.399 11.272 7.649 1.00 23.41 N ATOM 3181 CA ILE B 160 12.525 11.066 8.551 1.00 25.68 C ATOM 3182 C ILE B 160 13.758 10.625 7.764 1.00 28.19 C ATOM 3183 O ILE B 160 14.862 11.121 7.992 1.00 23.86 O ATOM 3184 CB ILE B 160 12.190 10.046 9.653 1.00 22.20 C ATOM 3185 CG1 ILE B 160 11.083 10.605 10.555 1.00 27.98 C ATOM 3186 CG2 ILE B 160 13.440 9.704 10.470 1.00 20.50 C ATOM 3187 CD1 ILE B 160 10.494 9.590 11.552 1.00 23.80 C ATOM 3188 N SER B 161 13.555 9.708 6.818 1.00 27.90 N ATOM 3189 CA SER B 161 14.656 9.215 6.002 1.00 28.39 C ATOM 3190 C SER B 161 15.225 10.324 5.143 1.00 23.70 C ATOM 3191 O SER B 161 16.435 10.451 5.052 1.00 22.04 O ATOM 3192 CB SER B 161 14.241 8.024 5.143 1.00 31.58 C ATOM 3193 OG SER B 161 14.013 6.875 5.936 1.00 32.14 O ATOM 3194 N ALA B 162 14.357 11.125 4.525 1.00 22.36 N ATOM 3195 CA ALA B 162 14.814 12.291 3.772 1.00 25.80 C ATOM 3196 C ALA B 162 15.566 13.274 4.672 1.00 25.71 C ATOM 3197 O ALA B 162 16.578 13.859 4.269 1.00 18.55 O ATOM 3198 CB ALA B 162 13.649 12.983 3.089 1.00 11.29 C ATOM 3199 N LEU B 163 15.064 13.450 5.892 1.00 20.35 N ATOM 3200 CA LEU B 163 15.645 14.421 6.802 1.00 22.30 C ATOM 3201 C LEU B 163 17.083 14.045 7.173 1.00 25.57 C ATOM 3202 O LEU B 163 17.993 14.865 7.052 1.00 21.94 O ATOM 3203 CB LEU B 163 14.792 14.576 8.058 1.00 24.55 C ATOM 3204 CG LEU B 163 15.319 15.590 9.088 1.00 28.46 C ATOM 3205 CD1 LEU B 163 15.348 17.008 8.520 1.00 25.41 C ATOM 3206 CD2 LEU B 163 14.506 15.562 10.352 1.00 23.26 C ATOM 3207 N VAL B 164 17.282 12.795 7.585 1.00 27.34 N ATOM 3208 CA VAL B 164 18.567 12.352 8.129 1.00 28.31 C ATOM 3209 C VAL B 164 19.617 11.907 7.117 1.00 31.69 C ATOM 3210 O VAL B 164 20.775 11.698 7.487 1.00 43.15 O ATOM 3211 CB VAL B 164 18.395 11.216 9.158 1.00 24.77 C ATOM 3212 CG1 VAL B 164 17.432 11.648 10.237 1.00 26.60 C ATOM 3213 CG2 VAL B 164 17.926 9.929 8.474 1.00 21.79 C ATOM 3214 N SER B 165 19.237 11.763 5.852 1.00 28.74 N ATOM 3215 CA SER B 165 20.192 11.262 4.859 1.00 32.18 C ATOM 3216 C SER B 165 20.137 11.884 3.470 1.00 28.79 C ATOM 3217 O SER B 165 21.110 11.823 2.732 1.00 42.76 O ATOM 3218 CB SER B 165 20.151 9.730 4.766 1.00 41.86 C ATOM 3219 OG SER B 165 18.848 9.214 4.939 1.00 47.47 O ATOM 3220 N PHE B 166 19.024 12.487 3.100 1.00 30.85 N ATOM 3221 CA PHE B 166 19.019 13.266 1.872 1.00 30.93 C ATOM 3222 C PHE B 166 19.571 14.676 2.124 1.00 26.66 C ATOM 3223 O PHE B 166 20.619 15.024 1.602 1.00 30.42 O ATOM 3224 CB PHE B 166 17.614 13.325 1.284 1.00 29.94 C ATOM 3225 CG PHE B 166 17.575 13.718 −0.156 1.00 23.56 C ATOM 3226 CD1 PHE B 166 17.395 15.041 −0.522 1.00 22.01 C ATOM 3227 CD2 PHE B 166 17.691 12.757 −1.145 1.00 30.21 C ATOM 3228 CE1 PHE B 166 17.346 15.400 −1.846 1.00 24.58 C ATOM 3229 CE2 PHE B 166 17.636 13.107 −2.481 1.00 29.24 C ATOM 3230 CZ PHE B 166 17.465 14.431 −2.830 1.00 34.78 C ATOM 3231 N LEU B 167 18.871 15.475 2.927 1.00 26.05 N ATOM 3232 CA LEU B 167 19.321 16.834 3.253 1.00 36.33 C ATOM 3233 C LEU B 167 20.830 17.031 3.531 1.00 35.42 C ATOM 3234 O LEU B 167 21.449 17.897 2.915 1.00 34.94 O ATOM 3235 CB LEU B 167 18.514 17.408 4.420 1.00 31.63 C ATOM 3236 CG LEU B 167 17.093 17.857 4.111 1.00 43.74 C ATOM 3237 CD1 LEU B 167 16.493 18.493 5.353 1.00 46.75 C ATOM 3238 CD2 LEU B 167 17.087 18.840 2.953 1.00 38.63 C ATOM 3239 N PRO B 168 21.413 16.253 4.473 1.00 31.97 N ATOM 3240 CA PRO B 168 22.809 16.482 4.863 1.00 31.19 C ATOM 3241 C PRO B 168 23.799 16.350 3.706 1.00 28.87 C ATOM 3242 O PRO B 168 24.742 17.146 3.595 1.00 24.60 O ATOM 3243 CB PRO B 168 23.061 15.381 5.899 1.00 25.80 C ATOM 3244 CG PRO B 168 21.730 15.036 6.414 1.00 21.17 C ATOM 3245 CD PRO B 168 20.814 15.156 5.252 1.00 27.03 C ATOM 3246 N ILE B 169 23.587 15.344 2.864 1.00 27.07 N ATOM 3247 CA ILE B 169 24.393 15.159 1.660 1.00 31.64 C ATOM 3248 C ILE B 169 24.237 16.323 0.689 1.00 29.97 C ATOM 3249 O ILE B 169 25.215 16.823 0.135 1.00 36.78 O ATOM 3250 CB ILE B 169 24.049 13.838 0.958 1.00 23.25 C ATOM 3251 CG1 ILE B 169 24.722 12.687 1.710 1.00 22.01 C ATOM 3252 CG2 ILE B 169 24.504 13.881 −0.483 1.00 19.29 C ATOM 3253 CD1 ILE B 169 24.291 11.317 1.320 1.00 17.36 C ATOM 3254 N MET B 170 23.001 16.759 0.501 1.00 23.63 N ATOM 3255 CA MET B 170 22.724 17.931 −0.312 1.00 29.18 C ATOM 3256 C MET B 170 23.114 19.255 0.364 1.00 37.27 C ATOM 3257 O MET B 170 23.206 20.283 −0.295 1.00 37.41 O ATOM 3258 CB MET B 170 21.253 17.940 −0.724 1.00 39.60 C ATOM 3259 CG MET B 170 20.835 16.715 −1.566 1.00 48.63 C ATOM 3260 SD MET B 170 21.160 16.861 −3.347 1.00 52.26 S ATOM 3261 CE MET B 170 22.931 16.602 −3.395 1.00 32.83 C ATOM 3262 N MET B 171 23.347 19.228 1.673 1.00 43.31 N ATOM 3263 CA MET B 171 23.838 20.405 2.397 1.00 41.88 C ATOM 3264 C MET B 171 25.369 20.418 2.467 1.00 37.87 C ATOM 3265 O MET B 171 25.975 21.376 2.940 1.00 28.19 O ATOM 3266 CB MET B 171 23.251 20.465 3.810 1.00 36.23 C ATOM 3267 CG MET B 171 21.826 21.028 3.910 1.00 44.09 C ATOM 3268 SD MET B 171 21.194 20.978 5.633 1.00 60.33 S ATOM 3269 CE MET B 171 21.954 22.444 6.320 1.00 36.27 C ATOM 3270 N HIS B 172 25.978 19.332 2.008 1.00 37.02 N ATOM 3271 CA HIS B 172 27.433 19.239 1.858 1.00 41.42 C ATOM 3272 C HIS B 172 28.193 18.988 3.142 1.00 26.86 C ATOM 3273 O HIS B 172 29.387 19.254 3.202 1.00 32.33 O ATOM 3274 CB HIS B 172 28.014 20.484 1.182 1.00 40.43 C ATOM 3275 CG HIS B 172 27.321 20.855 −0.090 1.00 50.66 C ATOM 3276 ND1 HIS B 172 27.412 20.092 −1.232 1.00 48.00 N ATOM 3277 CD2 HIS B 172 26.524 21.907 −0.393 1.00 47.54 C ATOM 3278 CE1 HIS B 172 26.700 20.662 −2.190 1.00 57.15 C ATOM 3279 NE2 HIS B 172 26.150 21.761 −1.709 1.00 52.67 N ATOM 3280 N TRP B 173 27.518 18.468 4.155 1.00 27.67 N ATOM 3281 CA TRP B 173 28.156 18.239 5.445 1.00 27.24 C ATOM 3282 C TRP B 173 29.097 17.032 5.406 1.00 34.23 C ATOM 3283 O TRP B 173 29.865 16.796 6.338 1.00 31.68 O ATOM 3284 CB TRP B 173 27.094 17.996 6.511 1.00 32.78 C ATOM 3285 CG TRP B 173 26.234 19.176 6.852 1.00 29.18 C ATOM 3286 CD1 TRP B 173 26.241 20.407 6.267 1.00 31.97 C ATOM 3287 CD2 TRP B 173 25.206 19.209 7.842 1.00 23.43 C ATOM 3288 NE1 TRP B 173 25.285 21.208 6.840 1.00 26.94 N ATOM 3289 CE2 TRP B 173 24.637 20.492 7.811 1.00 31.29 C ATOM 3290 CE3 TRP B 173 24.709 18.272 8.749 1.00 24.38 C ATOM 3291 CZ2 TRP B 173 23.602 20.864 8.663 1.00 34.07 C ATOM 3292 CZ3 TRP B 173 23.677 18.640 9.585 1.00 21.75 C ATOM 3293 CH2 TRP B 173 23.142 19.925 9.542 1.00 25.79 C ATOM 3294 N TRP B 174 29.021 16.263 4.329 1.00 27.35 N ATOM 3295 CA TRP B 174 29.763 15.018 4.222 1.00 25.08 C ATOM 3296 C TRP B 174 31.203 15.255 3.759 1.00 29.43 C ATOM 3297 O TRP B 174 32.015 14.328 3.743 1.00 27.85 O ATOM 3298 CB TRP B 174 29.051 14.071 3.242 1.00 29.47 C ATOM 3299 CG TRP B 174 28.915 14.659 1.846 1.00 32.12 C ATOM 3300 CD1 TRP B 174 27.998 15.582 1.431 1.00 29.68 C ATOM 3301 CD2 TRP B 174 29.735 14.375 0.706 1.00 26.16 C ATOM 3302 NE1 TRP B 174 28.197 15.890 0.113 1.00 30.04 N ATOM 3303 CE2 TRP B 174 29.259 15.164 −0.357 1.00 33.12 C ATOM 3304 CE3 TRP B 174 30.827 13.533 0.484 1.00 29.71 C ATOM 3305 CZ2 TRP B 174 29.830 15.130 −1.629 1.00 34.84 C ATOM 3306 CZ3 TRP B 174 31.392 13.502 −0.774 1.00 38.57 C ATOM 3307 CH2 TRP B 174 30.894 14.298 −1.816 1.00 31.02 C ATOM 3308 N ARG B 175 31.532 16.489 3.387 1.00 23.54 N ATOM 3309 CA ARG B 175 32.822 16.730 2.733 1.00 33.88 C ATOM 3310 C ARG B 175 34.022 16.825 3.669 1.00 33.51 C ATOM 3311 O ARG B 175 33.929 17.346 4.782 1.00 31.00 O ATOM 3312 CB ARG B 175 32.778 17.939 1.794 1.00 26.16 C ATOM 3313 CG ARG B 175 31.690 17.845 0.733 1.00 33.20 C ATOM 3314 CD ARG B 175 32.147 18.393 −0.601 1.00 32.36 C ATOM 3315 NE ARG B 175 31.266 19.446 −1.091 1.00 44.66 N ATOM 3316 CZ ARG B 175 30.894 19.585 −2.361 1.00 62.45 C ATOM 3317 NH1 ARG B 175 31.302 18.716 −3.275 1.00 55.21 N ATOM 3318 NH2 ARG B 175 30.089 20.580 −2.716 1.00 66.54 N ATOM 3319 N ASP B 176 35.148 16.314 3.182 1.00 29.66 N ATOM 3320 CA ASP B 176 36.412 16.346 3.894 1.00 29.09 C ATOM 3321 C ASP B 176 37.175 17.605 3.523 1.00 28.50 C ATOM 3322 O ASP B 176 36.738 18.364 2.677 1.00 31.32 O ATOM 3323 CB ASP B 176 37.234 15.110 3.546 1.00 41.23 C ATOM 3324 CG ASP B 176 38.171 14.704 4.662 1.00 53.28 C ATOM 3325 OD1 ASP B 176 38.533 15.579 5.477 1.00 48.28 O ATOM 3326 OD2 ASP B 176 38.540 13.506 4.722 1.00 66.48 O ATOM 3327 N GLU B 177 38.316 17.823 4.161 1.00 41.01 N ATOM 3328 CA GLU B 177 39.061 19.066 3.995 1.00 44.93 C ATOM 3329 C GLU B 177 40.357 18.786 3.248 1.00 50.53 C ATOM 3330 O GLU B 177 40.924 19.664 2.584 1.00 31.93 O ATOM 3331 CB GLU B 177 39.347 19.680 5.364 1.00 63.15 C ATOM 3332 CG GLU B 177 39.442 21.182 5.321 1.00 86.75 C ATOM 3333 CD GLU B 177 38.583 21.762 4.213 1.00 85.78 C ATOM 3334 OE1 GLU B 177 37.389 21.402 4.145 1.00 85.47 O ATOM 3335 OE2 GLU B 177 39.102 22.572 3.409 1.00 88.09 O ATOM 3336 N ASP B 178 40.782 17.530 3.366 1.00 46.54 N ATOM 3337 CA ASP B 178 41.948 16.950 2.699 1.00 45.18 C ATOM 3338 C ASP B 178 42.112 17.330 1.232 1.00 46.32 C ATOM 3339 O ASP B 178 41.133 17.395 0.491 1.00 54.70 O ATOM 3340 CB ASP B 178 41.847 15.423 2.789 1.00 48.19 C ATOM 3341 CG ASP B 178 43.134 14.725 2.403 1.00 65.42 C ATOM 3342 OD1 ASP B 178 44.223 15.252 2.718 1.00 69.89 O ATOM 3343 OD2 ASP B 178 43.061 13.635 1.797 1.00 73.91 O ATOM 3344 N PRO B 179 43.363 17.573 0.809 1.00 52.81 N ATOM 3345 CA PRO B 179 43.759 17.720 −0.595 1.00 50.10 C ATOM 3346 C PRO B 179 43.084 16.700 −1.525 1.00 47.27 C ATOM 3347 O PRO B 179 42.458 17.089 −2.520 1.00 33.85 O ATOM 3348 CB PRO B 179 45.267 17.456 −0.545 1.00 48.43 C ATOM 3349 CG PRO B 179 45.678 17.968 0.777 1.00 45.63 C ATOM 3350 CD PRO B 179 44.500 17.807 1.717 1.00 51.57 C ATOM 3351 N GLN B 180 43.221 15.413 −1.213 1.00 39.18 N ATOM 3352 CA GLN B 180 42.651 14.372 −2.059 1.00 42.14 C ATOM 3353 C GLN B 180 41.139 14.507 −2.214 1.00 42.79 C ATOM 3354 O GLN B 180 40.602 14.340 −3.311 1.00 37.64 O ATOM 3355 CB GLN B 180 43.011 12.987 −1.534 1.00 49.57 C ATOM 3356 CG GLN B 180 44.455 12.603 −1.798 1.00 78.53 C ATOM 3357 CD GLN B 180 44.756 11.162 −1.421 1.00 110.67 C ATOM 3358 OE1 GLN B 180 43.849 10.330 −1.319 1.00 115.43 O ATOM 3359 NE2 GLN B 180 46.036 10.858 −1.215 1.00 116.46 N ATOM 3360 N ALA B 181 40.459 14.810 −1.115 1.00 35.88 N ATOM 3361 CA ALA B 181 39.025 15.033 −1.153 1.00 33.81 C ATOM 3362 C ALA B 181 38.712 16.187 −2.097 1.00 36.68 C ATOM 3363 O ALA B 181 37.875 16.055 −2.994 1.00 33.02 O ATOM 3364 CB ALA B 181 38.482 15.313 0.243 1.00 34.53 C ATOM 3365 N LEU B 182 39.388 17.314 −1.907 1.00 34.70 N ATOM 3366 CA LEU B 182 39.147 18.485 −2.753 1.00 43.10 C ATOM 3367 C LEU B 182 39.403 18.189 −4.231 1.00 39.58 C ATOM 3368 O LEU B 182 38.674 18.661 −5.104 1.00 39.79 O ATOM 3369 CB LEU B 182 39.991 19.678 −2.292 1.00 49.61 C ATOM 3370 CG LEU B 182 39.541 20.315 −0.976 1.00 57.54 C ATOM 3371 CD1 LEU B 182 40.292 21.610 −0.738 1.00 56.18 C ATOM 3372 CD2 LEU B 182 38.030 20.549 −0.981 1.00 38.78 C ATOM 3373 N LYS B 183 40.441 17.403 −4.502 1.00 38.11 N ATOM 3374 CA LYS B 183 40.723 16.939 −5.853 1.00 36.86 C ATOM 3375 C LYS B 183 39.517 16.229 −6.441 1.00 35.27 C ATOM 3376 O LYS B 183 39.167 16.442 −7.592 1.00 33.65 O ATOM 3377 CB LYS B 183 41.912 15.986 −5.843 1.00 44.97 C ATOM 3378 CG LYS B 183 42.466 15.689 −7.207 1.00 39.35 C ATOM 3379 CD LYS B 183 43.814 15.019 −7.104 1.00 48.35 C ATOM 3380 CE LYS B 183 44.369 14.720 −8.486 1.00 63.07 C ATOM 3381 NZ LYS B 183 45.478 13.727 −8.423 1.00 84.28 N ATOM 3382 N CYS B 184 38.887 15.376 −5.641 1.00 36.46 N ATOM 3383 CA CYS B 184 37.739 14.609 −6.098 1.00 33.84 C ATOM 3384 C CYS B 184 36.537 15.503 −6.384 1.00 36.61 C ATOM 3385 O CYS B 184 35.858 15.349 −7.411 1.00 33.79 O ATOM 3386 CB CYS B 184 37.362 13.541 −5.070 1.00 33.65 C ATOM 3387 SG CYS B 184 35.999 12.453 −5.605 1.00 64.51 S ATOM 3388 N TYR B 185 36.273 16.434 −5.472 1.00 31.25 N ATOM 3389 CA TYR B 185 35.098 17.288 −5.599 1.00 34.98 C ATOM 3390 C TYR B 185 35.121 18.132 −6.876 1.00 36.81 C ATOM 3391 O TYR B 185 34.086 18.605 −7.341 1.00 36.62 O ATOM 3392 CB TYR B 185 34.926 18.181 −4.375 1.00 37.06 C ATOM 3393 CG TYR B 185 34.876 17.417 −3.078 1.00 37.46 C ATOM 3394 CD1 TYR B 185 34.389 16.115 −3.038 1.00 24.84 C ATOM 3395 CD2 TYR B 185 35.316 18.003 −1.883 1.00 28.18 C ATOM 3396 CE1 TYR B 185 34.358 15.408 −1.840 1.00 36.09 C ATOM 3397 CE2 TYR B 185 35.289 17.308 −0.689 1.00 25.25 C ATOM 3398 CZ TYR B 185 34.808 16.015 −0.664 1.00 29.55 C ATOM 3399 OH TYR B 185 34.765 15.324 0.527 1.00 26.04 O ATOM 3400 N GLN B 186 36.297 18.302 −7.457 1.00 38.65 N ATOM 3401 CA GLN B 186 36.406 19.127 −8.649 1.00 47.36 C ATOM 3402 C GLN B 186 36.527 18.336 −9.947 1.00 37.15 C ATOM 3403 O GLN B 186 36.475 18.900 −11.039 1.00 42.73 O ATOM 3404 CB GLN B 186 37.551 20.121 −8.506 1.00 45.51 C ATOM 3405 CG GLN B 186 37.144 21.346 −7.734 1.00 45.88 C ATOM 3406 CD GLN B 186 37.889 22.551 −8.200 1.00 70.74 C ATOM 3407 OE1 GLN B 186 38.516 22.528 −9.260 1.00 93.61 O ATOM 3408 NE2 GLN B 186 37.840 23.618 −7.415 1.00 94.50 N ATOM 3409 N ASP B 187 36.683 17.030 −9.823 1.00 28.21 N ATOM 3410 CA ASP B 187 36.701 16.176 −10.986 1.00 34.18 C ATOM 3411 C ASP B 187 35.291 15.633 −11.190 1.00 33.43 C ATOM 3412 O ASP B 187 34.823 14.834 −10.374 1.00 39.57 O ATOM 3413 CB ASP B 187 37.708 15.043 −10.781 1.00 33.95 C ATOM 3414 CG ASP B 187 37.787 14.090 −11.974 1.00 48.87 C ATOM 3415 OD1 ASP B 187 37.295 14.435 −13.078 1.00 42.99 O ATOM 3416 OD2 ASP B 187 38.349 12.983 −11.798 1.00 57.70 O ATOM 3417 N PRO B 188 34.597 16.091 −12.258 1.00 24.88 N ATOM 3418 CA PRO B 188 33.258 15.602 −12.601 1.00 24.83 C ATOM 3419 C PRO B 188 33.264 14.112 −12.864 1.00 26.40 C ATOM 3420 O PRO B 188 32.226 13.460 −12.787 1.00 34.03 O ATOM 3421 CB PRO B 188 32.919 16.369 −13.876 1.00 19.85 C ATOM 3422 CG PRO B 188 33.685 17.610 −13.784 1.00 19.23 C ATOM 3423 CD PRO B 188 34.971 17.251 −13.083 1.00 28.92 C ATOM 3424 N GLY B 189 34.438 13.576 −13.157 1.00 26.01 N ATOM 3425 CA GLY B 189 34.590 12.148 −13.329 1.00 29.28 C ATOM 3426 C GLY B 189 34.657 11.380 −12.020 1.00 25.49 C ATOM 3427 O GLY B 189 34.288 10.210 −11.968 1.00 34.11 O ATOM 3428 N CYS B 190 35.142 12.014 −10.960 1.00 24.21 N ATOM 3429 CA CYS B 190 35.222 11.332 −9.675 1.00 38.21 C ATOM 3430 C CYS B 190 33.900 11.396 −8.903 1.00 39.26 C ATOM 3431 O CYS B 190 33.380 12.489 −8.630 1.00 38.91 O ATOM 3432 CB CYS B 190 36.375 11.880 −8.835 1.00 30.13 C ATOM 3433 SG CYS B 190 36.492 11.184 −7.155 1.00 56.40 S ATOM 3434 N CYS B 191 33.354 10.218 −8.585 1.00 31.65 N ATOM 3435 CA CYS B 191 32.152 10.113 −7.752 1.00 38.91 C ATOM 3436 C CYS B 191 32.392 9.225 −6.532 1.00 39.92 C ATOM 3437 O CYS B 191 31.601 8.329 −6.246 1.00 47.76 O ATOM 3438 CB CYS B 191 30.939 9.601 −8.549 1.00 27.11 C ATOM 3439 SG CYS B 191 29.312 10.105 −7.836 1.00 35.39 S ATOM 3440 N ASP B 192 33.490 9.473 −5.823 1.00 46.50 N ATOM 3441 CA ASP B 192 33.793 8.744 −4.599 1.00 40.11 C ATOM 3442 C ASP B 192 33.089 9.422 −3.462 1.00 39.66 C ATOM 3443 O ASP B 192 33.142 10.645 −3.329 1.00 45.89 O ATOM 3444 CB ASP B 192 35.285 8.764 −4.289 1.00 38.06 C ATOM 3445 CG ASP B 192 36.094 7.968 −5.267 1.00 56.95 C ATOM 3446 OD1 ASP B 192 35.639 7.798 −6.417 1.00 65.13 O ATOM 3447 OD2 ASP B 192 37.200 7.527 −4.887 1.00 76.07 O ATOM 3448 N PHE B 193 32.433 8.632 −2.629 1.00 39.96 N ATOM 3449 CA PHE B 193 31.824 9.190 −1.436 1.00 40.43 C ATOM 3450 C PHE B 193 32.914 9.351 −0.365 1.00 35.27 C ATOM 3451 O PHE B 193 32.964 8.626 0.637 1.00 36.87 O ATOM 3452 CB PHE B 193 30.643 8.330 −0.972 1.00 27.56 C ATOM 3453 CG PHE B 193 29.669 9.068 −0.113 1.00 33.24 C ATOM 3454 CD1 PHE B 193 29.432 10.429 −0.325 1.00 23.81 C ATOM 3455 CD2 PHE B 193 28.981 8.405 0.904 1.00 25.58 C ATOM 3456 CE1 PHE B 193 28.529 11.118 0.458 1.00 21.82 C ATOM 3457 CE2 PHE B 193 28.087 9.081 1.690 1.00 27.28 C ATOM 3458 CZ PHE B 193 27.855 10.449 1.470 1.00 27.50 C ATOM 3459 N VAL B 194 33.802 10.307 −0.620 1.00 30.43 N ATOM 3460 CA VAL B 194 34.897 10.646 0.279 1.00 31.33 C ATOM 3461 C VAL B 194 34.396 11.602 1.341 1.00 30.10 C ATOM 3462 O VAL B 194 34.169 12.782 1.067 1.00 29.14 O ATOM 3463 CB VAL B 194 36.036 11.329 −0.503 1.00 31.58 C ATOM 3464 CG1 VAL B 194 37.131 11.823 0.448 1.00 28.55 C ATOM 3465 CG2 VAL B 194 36.587 10.378 −1.548 1.00 21.23 C ATOM 3466 N THR B 195 34.222 11.103 2.559 1.00 32.69 N ATOM 3467 CA THR B 195 33.554 11.896 3.596 1.00 33.28 C ATOM 3468 C THR B 195 34.462 12.196 4.767 1.00 30.39 C ATOM 3469 O THR B 195 35.440 11.481 5.000 1.00 44.74 O ATOM 3470 CB THR B 195 32.264 11.211 4.104 1.00 30.84 C ATOM 3471 OG1 THR B 195 32.582 9.943 4.689 1.00 28.03 O ATOM 3472 CG2 THR B 195 31.288 10.991 2.949 1.00 31.49 C ATOM 3473 N ASN B 196 34.148 13.259 5.499 1.00 28.76 N ATOM 3474 CA ASN B 196 34.856 13.516 6.745 1.00 32.00 C ATOM 3475 C ASN B 196 34.459 12.465 7.791 1.00 26.85 C ATOM 3476 O ASN B 196 33.366 11.891 7.721 1.00 26.63 O ATOM 3477 CB ASN B 196 34.622 14.950 7.228 1.00 28.61 C ATOM 3478 CG ASN B 196 33.188 15.202 7.654 1.00 28.63 C ATOM 3479 OD1 ASN B 196 32.667 14.544 8.547 1.00 29.84 O ATOM 3480 ND2 ASN B 196 32.557 16.180 7.035 1.00 26.35 N ATOM 3481 N ARG B 197 35.349 12.196 8.742 1.00 31.48 N ATOM 3482 CA ARG B 197 35.124 11.105 9.696 1.00 38.59 C ATOM 3483 C ARG B 197 33.928 11.323 10.636 1.00 29.75 C ATOM 3484 O ARG B 197 33.282 10.362 11.058 1.00 24.11 O ATOM 3485 CB ARG B 197 36.397 10.787 10.486 1.00 26.34 C ATOM 3486 CG ARG B 197 37.520 10.258 9.622 1.00 46.41 C ATOM 3487 CD ARG B 197 38.661 9.703 10.448 1.00 48.65 C ATOM 3488 NE ARG B 197 39.796 9.309 9.614 1.00 67.46 N ATOM 3489 CZ ARG B 197 40.915 8.754 10.080 1.00 89.84 C ATOM 3490 NH1 ARG B 197 41.063 8.518 11.381 1.00 96.11 N ATOM 3491 NH2 ARG B 197 41.891 8.431 9.245 1.00 91.14 N ATOM 3492 N ALA B 198 33.630 12.582 10.947 1.00 19.28 N ATOM 3493 CA ALA B 198 32.480 12.879 11.780 1.00 16.86 C ATOM 3494 C ALA B 198 31.246 12.347 11.089 1.00 29.06 C ATOM 3495 O ALA B 198 30.514 11.537 11.652 1.00 27.43 O ATOM 3496 CB ALA B 198 32.353 14.364 12.015 1.00 22.57 C ATOM 3497 N TYR B 199 31.044 12.781 9.845 1.00 32.96 N ATOM 3498 CA TYR B 199 29.864 12.411 9.083 1.00 20.39 C ATOM 3499 C TYR B 199 29.802 10.912 8.824 1.00 23.78 C ATOM 3500 O TYR B 199 28.720 10.327 8.806 1.00 27.29 O ATOM 3501 CB TYR B 199 29.780 13.198 7.777 1.00 26.17 C ATOM 3502 CG TYR B 199 28.713 12.662 6.858 1.00 27.90 C ATOM 3503 CD1 TYR B 199 27.491 13.307 6.719 1.00 29.01 C ATOM 3504 CD2 TYR B 199 28.917 11.480 6.156 1.00 25.29 C ATOM 3505 CE1 TYR B 199 26.512 12.796 5.884 1.00 28.40 C ATOM 3506 CE2 TYR B 199 27.958 10.963 5.340 1.00 27.93 C ATOM 3507 CZ TYR B 199 26.760 11.619 5.200 1.00 27.76 C ATOM 3508 OH TYR B 199 25.824 11.073 4.368 1.00 31.71 O ATOM 3509 N ALA B 200 30.953 10.280 8.625 1.00 26.87 N ATOM 3510 CA ALA B 200 30.963 8.828 8.423 1.00 36.15 C ATOM 3511 C ALA B 200 30.335 8.084 9.612 1.00 30.08 C ATOM 3512 O ALA B 200 29.521 7.189 9.433 1.00 26.22 O ATOM 3513 CB ALA B 200 32.369 8.330 8.167 1.00 21.71 C ATOM 3514 N ILE B 201 30.718 8.462 10.824 1.00 25.42 N ATOM 3515 CA ILE B 201 30.202 7.805 12.015 1.00 32.00 C ATOM 3516 C ILE B 201 28.750 8.191 12.338 1.00 28.76 C ATOM 3517 O ILE B 201 27.889 7.332 12.487 1.00 23.84 O ATOM 3518 CB ILE B 201 31.102 8.081 13.224 1.00 31.60 C ATOM 3519 CG1 ILE B 201 32.412 7.291 13.087 1.00 35.75 C ATOM 3520 CG2 ILE B 201 30.396 7.691 14.495 1.00 26.78 C ATOM 3521 CD1 ILE B 201 33.583 7.930 13.805 1.00 24.95 C ATOM 3522 N ALA B 202 28.484 9.487 12.428 1.00 23.11 N ATOM 3523 CA ALA B 202 27.152 9.958 12.740 1.00 22.93 C ATOM 3524 C ALA B 202 26.112 9.281 11.861 1.00 28.21 C ATOM 3525 O ALA B 202 25.120 8.746 12.362 1.00 29.74 O ATOM 3526 CB ALA B 202 27.066 11.480 12.612 1.00 19.08 C ATOM 3527 N SER B 203 26.356 9.281 10.556 1.00 26.21 N ATOM 3528 CA SER B 203 25.358 8.832 9.586 1.00 28.72 C ATOM 3529 C SER B 203 25.188 7.315 9.473 1.00 25.18 C ATOM 3530 O SER B 203 24.104 6.851 9.151 1.00 23.12 O ATOM 3531 CB SER B 203 25.616 9.438 8.203 1.00 25.52 C ATOM 3532 OG SER B 203 26.663 8.754 7.551 1.00 32.74 O ATOM 3533 N SER B 204 26.226 6.527 9.728 1.00 23.72 N ATOM 3534 CA SER B 204 25.993 5.078 9.745 1.00 34.76 C ATOM 3535 C SER B 204 25.224 4.656 10.996 1.00 32.22 C ATOM 3536 O SER B 204 24.301 3.839 10.926 1.00 30.64 O ATOM 3537 CB SER B 204 27.261 4.230 9.513 1.00 27.27 C ATOM 3538 OG SER B 204 28.438 4.989 9.623 1.00 37.04 O ATOM 3539 N ILE B 205 25.586 5.237 12.131 1.00 27.63 N ATOM 3540 CA ILE B 205 24.847 5.002 13.357 1.00 28.28 C ATOM 3541 C ILE B 205 23.377 5.384 13.208 1.00 34.25 C ATOM 3542 O ILE B 205 22.481 4.615 13.565 1.00 37.83 O ATOM 3543 CB ILE B 205 25.422 5.814 14.500 1.00 22.60 C ATOM 3544 CG1 ILE B 205 26.782 5.248 14.894 1.00 27.28 C ATOM 3545 CG2 ILE B 205 24.448 5.810 15.683 1.00 19.72 C ATOM 3546 CD1 ILE B 205 27.603 6.209 15.749 1.00 29.17 C ATOM 3547 N ILE B 206 23.140 6.577 12.672 1.00 29.75 N ATOM 3548 CA ILE B 206 21.801 7.161 12.594 1.00 22.22 C ATOM 3549 C ILE B 206 20.927 6.563 11.496 1.00 28.02 C ATOM 3550 O ILE B 206 19.722 6.431 11.659 1.00 31.41 O ATOM 3551 CB ILE B 206 21.899 8.680 12.372 1.00 20.83 C ATOM 3552 CG1 ILE B 206 22.323 9.363 13.666 1.00 33.25 C ATOM 3553 CG2 ILE B 206 20.597 9.246 11.881 1.00 24.46 C ATOM 3554 CD1 ILE B 206 22.514 10.843 13.528 1.00 40.23 C ATOM 3555 N SER B 207 21.539 6.212 10.368 1.00 37.02 N ATOM 3556 CA SER B 207 20.803 5.696 9.220 1.00 26.33 C ATOM 3557 C SER B 207 20.688 4.174 9.251 1.00 31.72 C ATOM 3558 O SER B 207 19.790 3.604 8.627 1.00 30.82 O ATOM 3559 CB SER B 207 21.459 6.146 7.903 1.00 27.46 C ATOM 3560 OG SER B 207 21.490 7.566 7.762 1.00 36.00 O ATOM 3561 N PHE B 208 21.587 3.519 9.983 1.00 28.52 N ATOM 3562 CA PHE B 208 21.653 2.063 9.979 1.00 27.99 C ATOM 3563 C PHE B 208 21.723 1.403 11.372 1.00 28.51 C ATOM 3564 O PHE B 208 20.868 0.591 11.702 1.00 30.41 O ATOM 3565 CB PHE B 208 22.812 1.604 9.075 1.00 29.07 C ATOM 3566 CG PHE B 208 22.892 0.110 8.881 1.00 31.13 C ATOM 3567 CD1 PHE B 208 22.111 −0.527 7.927 1.00 26.29 C ATOM 3568 CD2 PHE B 208 23.760 −0.657 9.651 1.00 33.70 C ATOM 3569 CE1 PHE B 208 22.194 −1.898 7.749 1.00 29.05 C ATOM 3570 CE2 PHE B 208 23.845 −2.035 9.482 1.00 30.79 C ATOM 3571 CZ PHE B 208 23.063 −2.654 8.531 1.00 33.65 C ATOM 3572 N TYR B 209 22.721 1.743 12.186 1.00 31.12 N ATOM 3573 CA TYR B 209 22.931 1.030 13.460 1.00 35.65 C ATOM 3574 C TYR B 209 21.767 1.069 14.433 1.00 33.44 C ATOM 3575 O TYR B 209 21.255 0.026 14.826 1.00 36.21 O ATOM 3576 CB TYR B 209 24.240 1.447 14.136 1.00 31.39 C ATOM 3577 CG TYR B 209 25.390 0.833 13.397 1.00 43.70 C ATOM 3578 CD1 TYR B 209 26.186 1.595 12.548 1.00 35.09 C ATOM 3579 CD2 TYR B 209 25.623 −0.535 13.474 1.00 35.22 C ATOM 3580 CE1 TYR B 209 27.210 1.023 11.832 1.00 30.85 C ATOM 3581 CE2 TYR B 209 26.649 −1.117 12.763 1.00 42.15 C ATOM 3582 CZ TYR B 209 27.439 −0.337 11.943 1.00 38.40 C ATOM 3583 OH TYR B 209 28.460 −0.934 11.245 1.00 35.90 O ATOM 3584 N ILE B 210 21.353 2.269 14.812 1.00 31.77 N ATOM 3585 CA ILE B 210 20.180 2.439 15.660 1.00 35.13 C ATOM 3586 C ILE B 210 18.948 1.694 15.147 1.00 34.58 C ATOM 3587 O ILE B 210 18.384 0.863 15.866 1.00 31.66 O ATOM 3588 CB ILE B 210 19.833 3.919 15.830 1.00 29.49 C ATOM 3589 CG1 ILE B 210 20.835 4.575 16.777 1.00 24.87 C ATOM 3590 CG2 ILE B 210 18.397 4.073 16.319 1.00 30.97 C ATOM 3591 CD1 ILE B 210 20.784 6.078 16.729 1.00 34.98 C ATOM 3592 N PRO B 211 18.522 1.989 13.904 1.00 34.83 N ATOM 3593 CA PRO B 211 17.340 1.291 13.387 1.00 32.09 C ATOM 3594 C PRO B 211 17.563 −0.208 13.345 1.00 32.70 C ATOM 3595 O PRO B 211 16.602 −0.968 13.402 1.00 36.41 O ATOM 3596 CB PRO B 211 17.208 1.826 11.969 1.00 23.58 C ATOM 3597 CG PRO B 211 17.926 3.133 11.983 1.00 27.75 C ATOM 3598 CD PRO B 211 19.056 2.961 12.935 1.00 28.27 C ATOM 3599 N LEU B 212 18.816 −0.634 13.265 1.00 27.34 N ATOM 3600 CA LEU B 212 19.093 −2.055 13.159 1.00 31.54 C ATOM 3601 C LEU B 212 18.958 −2.725 14.509 1.00 39.16 C ATOM 3602 O LEU B 212 18.290 −3.748 14.652 1.00 36.88 O ATOM 3603 CB LEU B 212 20.489 −2.304 12.618 1.00 32.85 C ATOM 3604 CG LEU B 212 20.680 −3.810 12.539 1.00 33.38 C ATOM 3605 CD1 LEU B 212 20.072 −4.295 11.251 1.00 32.29 C ATOM 3606 CD2 LEU B 212 22.140 −4.201 12.660 1.00 33.74 C ATOM 3607 N LEU B 213 19.617 −2.147 15.502 1.00 37.23 N ATOM 3608 CA LEU B 213 19.480 −2.626 16.861 1.00 32.79 C ATOM 3609 C LEU B 213 18.006 −2.744 17.211 1.00 36.53 C ATOM 3610 O LEU B 213 17.531 −3.843 17.472 1.00 3.7.95 O ATOM 3611 CB LEU B 213 20.226 −1.707 17.816 1.00 31.98 C ATOM 3612 CG LEU B 213 21.694 −1.670 17.383 1.00 43.51 C ATOM 3613 CD1 LEU B 213 22.561 −0.762 18.252 1.00 38.20 C ATOM 3614 CD2 LEU B 213 22.246 −3.093 17.356 1.00 37.60 C ATOM 3615 N ILE B 214 17.277 −1.629 17.172 1.00 35.82 N ATOM 3616 CA ILE B 214 15.849 −1.642 17.487 1.00 34.50 C ATOM 3617 C ILE B 214 15.142 −2.795 16.782 1.00 40.13 C ATOM 3618 O ILE B 214 14.441 −3.581 17.411 1.00 42.45 O ATOM 3619 CB ILE B 214 15.153 −0.325 17.106 1.00 31.60 C ATOM 3620 CG1 ILE B 214 15.521 0.780 18.087 1.00 24.13 C ATOM 3621 CG2 ILE B 214 13.632 −0.491 17.108 1.00 26.92 C ATOM 3622 CD1 ILE B 214 15.146 2.158 17.574 1.00 23.20 C ATOM 3623 N MET B 215 15.332 −2.907 15.477 1.00 33.41 N ATOM 3624 CA MET B 215 14.655 −3.960 14.744 1.00 39.32 C ATOM 3625 C MET B 215 15.044 −5.343 15.232 1.00 42.70 C ATOM 3626 O MET B 215 14.211 −6.239 15.282 1.00 44.83 O ATOM 3627 CB MET B 215 14.941 −3.887 13.251 1.00 47.17 C ATOM 3628 CG MET B 215 14.268 −5.023 12.504 1.00 50.64 C ATOM 3629 SD MET B 215 14.968 −5.323 10.887 1.00 55.93 S ATOM 3630 CE MET B 215 16.609 −5.867 11.337 1.00 38.75 C ATOM 3631 N ILE B 216 16.315 −5.522 15.567 1.00 47.13 N ATOM 3632 CA ILE B 216 16.805 −6.828 15.992 1.00 45.31 C ATOM 3633 C ILE B 216 16.153 −7.232 17.311 1.00 47.08 C ATOM 3634 O ILE B 216 15.614 −8.331 17.431 1.00 44.99 O ATOM 3635 CB ILE B 216 18.352 −6.851 16.090 1.00 54.97 C ATOM 3636 CG1 ILE B 216 18.963 −7.205 14.725 1.00 54.55 C ATOM 3637 CG2 ILE B 216 18.822 −7.838 17.157 1.00 45.21 C ATOM 3638 CD1 ILE B 216 20.450 −6.878 14.588 1.00 43.41 C ATOM 3639 N PHE B 217 16.197 −6.320 18.278 1.00 47.45 N ATOM 3640 CA PHE B 217 15.571 −6.484 19.588 1.00 44.77 C ATOM 3641 C PHE B 217 14.080 −6.792 19.451 1.00 48.75 C ATOM 3642 O PHE B 217 13.635 −7.915 19.704 1.00 49.23 O ATOM 3643 CB PHE B 217 15.794 −5.198 20.398 1.00 47.14 C ATOM 3644 CG PHE B 217 15.130 −5.180 21.757 1.00 73.92 C ATOM 3645 CD1 PHE B 217 15.868 −5.428 22.911 1.00 72.76 C ATOM 3646 CD2 PHE B 217 13.779 −4.861 21.889 1.00 67.29 C ATOM 3647 CE1 PHE B 217 15.261 −5.392 24.167 1.00 74.63 C ATOM 3648 CE2 PHE B 217 13.169 −4.823 23.142 1.00 57.41 C ATOM 3649 CZ PHE B 217 13.909 −5.089 24.279 1.00 63.47 C ATOM 3650 N VAL B 218 13.316 −5.790 19.038 1.00 47.45 N ATOM 3651 CA VAL B 218 11.873 −5.923 18.901 1.00 38.01 C ATOM 3652 C VAL B 218 11.535 −7.227 18.187 1.00 38.38 C ATOM 3653 O VAL B 218 10.567 −7.899 18.530 1.00 46.50 O ATOM 3654 CB VAL B 218 11.273 −4.693 18.166 1.00 35.28 C ATOM 3655 CG1 VAL B 218 9.811 −4.910 17.803 1.00 30.61 C ATOM 3656 CG2 VAL B 218 11.449 −3.435 19.019 1.00 27.70 C ATOM 3657 N ALA B 219 12.355 −7.598 17.215 1.00 36.89 N ATOM 3658 CA ALA B 219 12.123 −8.812 16.444 1.00 42.43 C ATOM 3659 C ALA B 219 12.294 −10.069 17.286 1.00 51.60 C ATOM 3660 O ALA B 219 11.493 −10.996 17.190 1.00 54.50 O ATOM 3661 CB ALA B 219 13.043 −8.862 15.241 1.00 41.27 C ATOM 3662 N LEU B 220 13.344 −10.111 18.097 1.00 47.34 N ATOM 3663 CA LEU B 220 13.565 −11.251 18.973 1.00 48.94 C ATOM 3664 C LEU B 220 12.377 −11.423 19.907 1.00 58.20 C ATOM 3665 O LEU B 220 11.912 −12.539 20.136 1.00 57.79 O ATOM 3666 CB LEU B 220 14.860 −11.085 19.767 1.00 46.53 C ATOM 3667 CG LEU B 220 16.119 −11.234 18.907 1.00 58.64 C ATOM 3668 CD1 LEU B 220 17.363 −10.833 19.678 1.00 47.59 C ATOM 3669 CD2 LEU B 220 16.242 −12.656 18.357 1.00 43.62 C ATOM 3670 N ARG B 221 11.875 −10.308 20.425 1.00 44.87 N ATOM 3671 CA ARG B 221 10.718 −10.338 21.305 1.00 49.56 C ATOM 3672 C ARG B 221 9.537 −11.037 20.641 1.00 60.06 C ATOM 3673 O ARG B 221 8.938 −11.950 21.212 1.00 62.85 O ATOM 3674 CB ARG B 221 10.326 −8.920 21.725 1.00 58.87 C ATOM 3675 CG ARG B 221 11.290 −8.275 22.711 1.00 59.77 C ATOM 3676 CD ARG B 221 11.163 −8.895 24.090 1.00 84.85 C ATOM 3677 NE ARG B 221 12.215 −8.449 25.000 1.00 109.64 N ATOM 3678 CZ ARG B 221 12.251 −8.740 26.299 1.00 128.22 C ATOM 3679 NH1 ARG B 221 11.288 −9.476 26.842 1.00 127.61 N ATOM 3680 NH2 ARG B 221 13.247 −8.296 27.058 1.00 119.15 N ATOM 3681 N VAL B 222 9.201 −10.605 19.432 1.00 61.50 N ATOM 3682 CA VAL B 222 8.106 −11.214 18.692 1.00 53.88 C ATOM 3683 C VAL B 222 8.268 −12.729 18.587 1.00 58.23 C ATOM 3684 O VAL B 222 7.281 −13.464 18.599 1.00 56.04 O ATOM 3685 CB VAL B 222 7.986 −10.609 17.295 1.00 43.18 C ATOM 3686 CG1 VAL B 222 6.887 −11.311 16.499 1.00 45.51 C ATOM 3687 CG2 VAL B 222 7.713 −9.120 17.405 1.00 43.31 C ATOM 3688 N TYR B 223 9.512 −13.194 18.499 1.00 62.09 N ATOM 3689 CA TYR B 223 9.773 −14.628 18.402 1.00 69.09 C ATOM 3690 C TYR B 223 9.394 −15.348 19.687 1.00 65.03 C ATOM 3691 O TYR B 223 8.723 −16.374 19.657 1.00 66.56 O ATOM 3692 CB TYR B 223 11.239 −14.903 18.079 1.00 65.47 C ATOM 3693 CG TYR B 223 11.513 −16.356 17.760 1.00 69.06 C ATOM 3694 CD1 TYR B 223 10.976 −16.944 16.626 1.00 74.10 C ATOM 3695 CD2 TYR B 223 12.308 −17.139 18.589 1.00 76.99 C ATOM 3696 CE1 TYR B 223 11.221 −18.271 16.322 1.00 88.31 C ATOM 3697 CE2 TYR B 223 12.561 −18.469 18.292 1.00 83.75 C ATOM 3698 CZ TYR B 223 12.014 −19.028 17.159 1.00 86.98 C ATOM 3699 OH TYR B 223 12.259 −20.348 16.860 1.00 94.51 O ATOM 3700 N ARG B 224 9.841 −14.810 20.815 1.00 63.26 N ATOM 3701 CA ARG B 224 9.526 −15.406 22.105 1.00 70.75 C ATOM 3702 C ARG B 224 8.023 −15.430 22.299 1.00 73.98 C ATOM 3703 O ARG B 224 7.470 −16.417 22.778 1.00 77.48 O ATOM 3704 CB ARG B 224 10.224 −14.651 23.240 1.00 60.44 C ATOM 3705 CG ARG B 224 11.721 −14.928 23.294 1.00 76.25 C ATOM 3706 CD ARG B 224 12.499 −13.882 24.077 1.00 86.71 C ATOM 3707 NE ARG B 224 13.928 −13.972 23.775 1.00 101.98 N ATOM 3708 CZ ARG B 224 14.889 −13.372 24.472 1.00 108.15 C ATOM 3709 NH1 ARG B 224 14.584 −12.632 25.528 1.00 107.44 N ATOM 3710 NH2 ARG B 224 16.161 −13.518 24.116 1.00 95.70 N ATOM 3711 N GLU B 225 7.368 −14.348 21.893 1.00 70.71 N ATOM 3712 CA GLU B 225 5.921 −14.239 22.009 1.00 70.98 C ATOM 3713 C GLU B 225 5.187 −15.268 21.171 1.00 72.14 C ATOM 3714 O GLU B 225 4.176 −15.816 21.599 1.00 85.72 O ATOM 3715 CB GLU B 225 5.457 −12.836 21.629 1.00 71.19 C ATOM 3716 CG GLU B 225 5.481 −11.877 22.793 1.00 86.76 C ATOM 3717 CD GLU B 225 4.663 −12.387 23.965 1.00 107.93 C ATOM 3718 OE1 GLU B 225 3.746 −13.210 23.735 1.00 107.13 O ATOM 3719 OE2 GLU B 225 4.938 −11.966 25.110 1.00 103.05 O ATOM 3720 N ALA B 226 5.688 −15.524 19.971 1.00 74.32 N ATOM 3721 CA ALA B 226 5.055 −16.495 19.095 1.00 81.63 C ATOM 3722 C ALA B 226 5.204 −17.896 19.685 1.00 89.58 C ATOM 3723 O ALA B 226 4.307 −18.730 19.552 1.00 94.07 O ATOM 3724 CB ALA B 226 5.648 −16.421 17.698 1.00 72.68 C ATOM 3725 N LYS B 227 6.335 −18.138 20.346 1.00 85.80 N ATOM 3726 CA LYS B 227 6.598 −19.411 21.014 1.00 78.60 C ATOM 3727 C LYS B 227 5.703 −19.595 22.240 1.00 86.72 C ATOM 3728 O LYS B 227 5.087 −20.645 22.414 1.00 78.06 O ATOM 3729 CB LYS B 227 8.065 −19.506 21.428 1.00 73.56 C ATOM 3730 CG LYS B 227 8.997 −19.991 20.334 1.00 88.25 C ATOM 3731 CD LYS B 227 10.375 −20.337 20.897 1.00 90.70 C ATOM 3732 CE LYS B 227 11.196 −21.153 19.902 1.00 100.25 C ATOM 3733 NZ LYS B 227 12.507 −21.583 20.464 1.00 95.71 N ATOM 3734 N GLU B 228 5.645 −18.569 23.088 1.00 91.92 N ATOM 3735 CA GLU B 228 4.778 −18.573 24.268 1.00 87.75 C ATOM 3736 C GLU B 228 3.318 −18.715 23.880 1.00 79.54 C ATOM 3737 O GLU B 228 2.444 −18.724 24.740 1.00 88.05 O ATOM 3738 CB GLU B 228 4.934 −17.282 25.078 1.00 91.26 C ATOM 3739 CG GLU B 228 6.223 −17.160 25.874 1.00 109.19 C ATOM 3740 CD GLU B 228 6.343 −15.815 26.583 1.00 119.86 C ATOM 3741 OE1 GLU B 228 5.388 −15.420 27.288 1.00 109.43 O ATOM 3742 OE2 GLU B 228 7.395 −15.153 26.435 1.00 121.55 O ATOM 3743 N GLN B 229 3.055 −18.800 22.582 1.00 94.93 N ATOM 3744 CA GLN B 229 1.701 −19.015 22.092 1.00 91.19 C ATOM 3745 C GLN B 229 1.507 −20.458 21.652 1.00 89.25 C ATOM 3746 O GLN B 229 0.405 −20.996 21.751 1.00 93.53 O ATOM 3747 CB GLN B 229 1.382 −18.070 20.934 1.00 84.10 C ATOM 3748 CG GLN B 229 0.954 −16.680 21.370 1.00 86.84 C ATOM 3749 CD GLN B 229 0.451 −15.833 20.213 1.00 101.43 C ATOM 3750 OE1 GLN B 229 −0.259 −14.847 20.416 1.00 93.37 O ATOM 3751 NE2 GLN B 229 0.814 −16.216 18.991 1.00 101.10 N ATOM 3752 N ILE B 230 2.589 −21.080 21.190 1.00 83.18 N ATOM 3753 CA ILE B 230 2.534 −22.385 20.540 1.00 99.88 C ATOM 3754 C ILE B 230 3.495 −22.363 19.377 1.00 108.13 C ATOM 3755 O ILE B 230 4.701 −22.564 19.512 1.00 108.13 O ATOM 3756 CB ILE B 230 1.194 −22.604 19.842 1.00 115.38 C ATOM 3757 CG1 ILE B 230 1.265 −23.850 18.965 1.00 111.77 C ATOM 3758 CG2 ILE B 230 0.879 −21.424 18.921 1.00 112.34 C ATOM 3759 CD1 ILE B 230 0.799 −23.604 17.540 1.00 114.10 C ATOM 3760 N ARG B 267 −1.226 −20.535 10.457 1.00 96.06 N ATOM 3761 CA ARG B 267 −0.491 −20.193 9.249 1.00 101.47 C ATOM 3762 C ARG B 267 0.211 −18.866 9.479 1.00 106.58 C ATOM 3763 O ARG B 267 1.174 −18.532 8.788 1.00 97.73 O ATOM 3764 CB ARG B 267 −1.446 −20.047 8.062 1.00 112.42 C ATOM 3765 CG ARG B 267 −2.012 −21.356 7.528 1.00 136.64 C ATOM 3766 CD ARG B 267 −1.025 −22.075 6.604 1.00 140.65 C ATOM 3767 NE ARG B 267 −1.454 −23.441 6.304 1.00 151.36 N ATOM 3768 CZ ARG B 267 −0.753 −24.310 5.580 1.00 137.07 C ATOM 3769 NH1 ARG B 267 0.420 −23.960 5.070 1.00 134.64 N ATOM 3770 NH2 ARG B 267 −1.226 −25.531 5.366 1.00 112.52 N ATOM 3771 N GLU B 268 −0.289 −18.114 10.457 1.00 112.19 N ATOM 3772 CA GLU B 268 0.214 −16.778 10.770 1.00 98.22 C ATOM 3773 C GLU B 268 1.711 −16.776 11.044 1.00 89.25 C ATOM 3774 O GLU B 268 2.383 −15.762 10.867 1.00 77.50 O ATOM 3775 CB GLU B 268 −0.522 −16.206 11.984 1.00 106.43 C ATOM 3776 CG GLU B 268 −2.037 −16.287 11.894 1.00 121.11 C ATOM 3777 CD GLU B 268 −2.606 −15.421 10.785 1.00 135.87 C ATOM 3778 OE1 GLU B 268 −1.839 −14.625 10.199 1.00 136.35 O ATOM 3779 OE2 GLU B 268 −3.820 −15.536 10.502 1.00 119.82 O ATOM 3780 N HIS B 269 2.229 −17.916 11.483 1.00 84.80 N ATOM 3781 CA HIS B 269 3.646 −18.034 11.786 1.00 85.68 C ATOM 3782 C HIS B 269 4.515 −18.086 10.530 1.00 79.97 C ATOM 3783 O HIS B 269 5.610 −17.522 10.496 1.00 66.05 O ATOM 3784 CB HIS B 269 3.883 −19.248 12.674 1.00 93.90 C ATOM 3785 CG HIS B 269 3.413 −19.049 14.078 1.00 101.11 C ATOM 3786 ND1 HIS B 269 4.181 −19.378 15.175 1.00 109.47 N ATOM 3787 CD2 HIS B 269 2.266 −18.523 14.564 1.00 100.55 C ATOM 3788 CE1 HIS B 269 3.516 −19.081 16.277 1.00 105.55 C ATOM 3789 NE2 HIS B 269 2.352 −18.559 15.935 1.00 106.90 N ATOM 3790 N LYS B 270 4.029 −18.763 9.498 1.00 86.37 N ATOM 3791 CA LYS B 270 4.736 −18.780 8.226 1.00 84.00 C ATOM 3792 C LYS B 270 4.881 −17.343 7.745 1.00 77.23 C ATOM 3793 O LYS B 270 5.943 −16.946 7.259 1.00 68.91 O ATOM 3794 CB LYS B 270 3.993 −19.639 7.199 1.00 84.96 C ATOM 3795 CG LYS B 270 3.904 −21.104 7.605 1.00 107.28 C ATOM 3796 CD LYS B 270 2.896 −21.876 6.771 1.00 117.71 C ATOM 3797 CE LYS B 270 2.635 −23.252 7.372 1.00 116.08 C ATOM 3798 NZ LYS B 270 3.905 −23.972 7.692 1.00 116.51 N ATOM 3799 N ALA B 271 3.814 −16.563 7.907 1.00 77.57 N ATOM 3800 CA ALA B 271 3.839 −15.145 7.559 1.00 67.05 C ATOM 3801 C ALA B 271 4.863 −14.415 8.413 1.00 55.60 C ATOM 3802 O ALA B 271 5.664 −13.641 7.907 1.00 47.53 O ATOM 3803 CB ALA B 271 2.461 −14.517 7.722 1.00 57.67 C ATOM 3804 N LEU B 272 4.844 −14.667 9.714 1.00 61.55 N ATOM 3805 CA LEU B 272 5.838 −14.060 10.587 1.00 64.62 C ATOM 3806 C LEU B 272 7.233 −14.498 10.164 1.00 54.33 C ATOM 3807 O LEU B 272 8.127 −13.670 10.019 1.00 50.35 O ATOM 3808 CB LEU B 272 5.582 −14.406 12.055 1.00 69.03 C ATOM 3809 CG LEU B 272 4.378 −13.733 12.713 1.00 65.85 C ATOM 3810 CD1 LEU B 272 4.467 −13.888 14.217 1.00 58.80 C ATOM 3811 CD2 LEU B 272 4.295 −12.265 12.324 1.00 51.47 C ATOM 3812 N LYS B 273 7.407 −15.796 9.940 1.00 58.17 N ATOM 3813 CA LYS B 273 8.718 −16.322 9.589 1.00 62.15 C ATOM 3814 C LYS B 273 9.270 −15.662 8.326 1.00 55.97 C ATOM 3815 O LYS B 273 10.438 −15.277 8.277 1.00 52.96 O ATOM 3816 CB LYS B 273 8.691 −17.844 9.424 1.00 66.21 C ATOM 3817 CG LYS B 273 10.081 −18.463 9.524 1.00 74.02 C ATOM 3818 CD LYS B 273 10.201 −19.782 8.774 1.00 70.37 C ATOM 3819 CE LYS B 273 11.612 −20.344 8.911 1.00 74.14 C ATOM 3820 NZ LYS B 273 11.847 −21.513 8.020 1.00 87.37 N ATOM 3821 N THR B 274 8.429 −15.540 7.307 1.00 50.23 N ATOM 3822 CA THR B 274 8.819 −14.846 6.088 1.00 57.86 C ATOM 3823 C THR B 274 9.369 −13.458 6.411 1.00 48.75 C ATOM 3824 O THR B 274 10.401 −13.066 5.879 1.00 41.76 O ATOM 3825 CB THR B 274 7.639 −14.704 5.091 1.00 61.90 C ATOM 3826 OG1 THR B 274 7.359 −15.969 4.476 1.00 65.03 O ATOM 3827 CG2 THR B 274 7.972 −13.693 4.009 1.00 49.82 C ATOM 3828 N LEU B 275 8.681 −12.726 7.285 1.00 43.51 N ATOM 3829 CA LEU B 275 9.113 −11.381 7.661 1.00 44.80 C ATOM 3830 C LEU B 275 10.480 −11.397 8.327 1.00 46.43 C ATOM 3831 O LEU B 275 11.296 −10.511 8.093 1.00 50.55 O ATOM 3832 CB LEU B 275 8.101 −10.705 8.582 1.00 29.73 C ATOM 3833 CG LEU B 275 6.699 −10.550 7.991 1.00 44.30 C ATOM 3834 CD1 LEU B 275 5.759 −9.850 8.963 1.00 32.32 C ATOM 3835 CD2 LEU B 275 6.744 −9.817 6.656 1.00 38.16 C ATOM 3836 N GLY B 276 10.730 −12.406 9.154 1.00 44.84 N ATOM 3837 CA GLY B 276 12.011 −12.531 9.824 1.00 36.72 C ATOM 3838 C GLY B 276 13.102 −12.808 8.817 1.00 43.08 C ATOM 3839 O GLY B 276 14.239 −12.384 8.985 1.00 49.88 O ATOM 3840 N ILE B 277 12.749 −13.525 7.759 1.00 40.22 N ATOM 3841 CA ILE B 277 13.701 −13.835 6.705 1.00 46.75 C ATOM 3842 C ILE B 277 14.024 −12.592 5.866 1.00 44.30 C ATOM 3843 O ILE B 277 15.189 −12.330 5.572 1.00 46.53 O ATOM 3844 CB ILE B 277 13.193 −14.989 5.821 1.00 51.66 C ATOM 3845 CG1 ILE B 277 13.145 −16.287 6.635 1.00 42.99 C ATOM 3846 CG2 ILE B 277 14.073 −15.149 4.584 1.00 35.39 C ATOM 3847 CD1 ILE B 277 12.426 −17.421 5.930 1.00 45.89 C ATOM 3848 N ILE B 278 12.990 −11.841 5.488 1.00 41.57 N ATOM 3849 CA ILE B 278 13.146 −10.525 4.871 1.00 32.71 C ATOM 3850 C ILE B 278 14.170 −9.709 5.653 1.00 43.54 C ATOM 3851 O ILE B 278 15.087 −9.105 5.075 1.00 36.40 O ATOM 3852 CB ILE B 278 11.809 −9.749 4.880 1.00 34.70 C ATOM 3853 CG1 ILE B 278 10.792 −10.408 3.955 1.00 42.37 C ATOM 3854 CG2 ILE B 278 11.996 −8.307 4.487 1.00 39.51 C ATOM 3855 CD1 ILE B 278 11.375 −10.942 2.690 1.00 46.62 C ATOM 3856 N MET B 279 14.012 −9.715 6.976 1.00 37.92 N ATOM 3857 CA MET B 279 14.860 −8.934 7.873 1.00 40.68 C ATOM 3858 C MET B 279 16.279 −9.482 7.974 1.00 42.25 C ATOM 3859 O MET B 279 17.240 −8.718 7.924 1.00 46.61 O ATOM 3860 CB MET B 279 14.245 −8.844 9.275 1.00 43.21 C ATOM 3861 CG MET B 279 12.937 −8.053 9.361 1.00 44.30 C ATOM 3862 SD MET B 279 12.231 −8.091 11.036 1.00 63.24 S ATOM 3863 CE MET B 279 10.533 −7.622 10.708 1.00 35.00 C ATOM 3864 N GLY B 280 16.411 −10.797 8.129 1.00 35.75 N ATOM 3865 CA GLY B 280 17.716 −11.405 8.322 1.00 36.73 C ATOM 3866 C GLY B 280 18.584 −11.305 7.080 1.00 44.40 C ATOM 3867 O GLY B 280 19.796 −11.043 7.146 1.00 32.64 O ATOM 3868 N VAL B 281 17.956 −11.525 5.933 1.00 35.68 N ATOM 3869 CA VAL B 281 18.642 −11.357 4.669 1.00 39.95 C ATOM 3870 C VAL B 281 19.064 −9.899 4.512 1.00 40.12 C ATOM 3871 O VAL B 281 20.137 −9.618 3.987 1.00 34.12 O ATOM 3872 CB VAL B 281 17.766 −11.790 3.463 1.00 47.59 C ATOM 3873 CG1 VAL B 281 18.310 −11.200 2.160 1.00 39.24 C ATOM 3874 CG2 VAL B 281 17.694 −13.302 3.367 1.00 39.47 C ATOM 3875 N PHE B 282 18.227 −8.968 4.966 1.00 37.18 N ATOM 3876 CA PHE B 282 18.591 −7.566 4.844 1.00 32.78 C ATOM 3877 C PHE B 282 19.865 −7.304 5.626 1.00 41.43 C ATOM 3878 O PHE B 282 20.791 −6.658 5.127 1.00 40.28 O ATOM 3879 CB PHE B 282 17.486 −6.638 5.338 1.00 32.12 C ATOM 3880 CG PHE B 282 17.860 −5.183 5.274 1.00 36.54 C ATOM 3881 CD1 PHE B 282 17.526 −4.416 4.169 1.00 35.77 C ATOM 3882 CD2 PHE B 282 18.577 −4.585 6.310 1.00 36.56 C ATOM 3883 CE1 PHE B 282 17.882 −3.076 4.100 1.00 28.88 C ATOM 3884 CE2 PHE B 282 18.945 −3.246 6.240 1.00 30.42 C ATOM 3885 CZ PHE B 282 18.594 −2.490 5.138 1.00 23.23 C ATOM 3886 N THR B 283 19.908 −7.813 6.853 1.00 33.73 N ATOM 3887 CA THR B 283 21.026 −7.553 7.746 1.00 31.18 C ATOM 3888 C THR B 283 22.295 −8.186 7.209 1.00 37.31 C ATOM 3889 O THR B 283 23.375 −7.608 7.304 1.00 41.40 O ATOM 3890 CB THR B 283 20.748 −8.073 9.165 1.00 35.55 C ATOM 3891 OG1 THR B 283 19.550 −7.466 9.662 1.00 41.76 O ATOM 3892 CG2 THR B 283 21.900 −7.739 10.104 1.00 27.01 C ATOM 3893 N LEU B 284 22.163 −9.378 6.643 1.00 42.06 N ATOM 3894 CA LEU B 284 23.310 −10.078 6.083 1.00 42.65 C ATOM 3895 C LEU B 284 23.874 −9.336 4.876 1.00 41.90 C ATOM 3896 O LEU B 284 25.086 −9.202 4.736 1.00 42.14 O ATOM 3897 CB LEU B 284 22.918 −11.504 5.703 1.00 49.08 C ATOM 3898 CG LEU B 284 22.992 −12.500 6.860 1.00 62.77 C ATOM 3899 CD1 LEU B 284 22.071 −13.706 6.654 1.00 46.73 C ATOM 3900 CD2 LEU B 284 24.438 −12.926 7.048 1.00 54.04 C ATOM 3901 N CYS B 285 22.984 −8.845 4.020 1.00 35.56 N ATOM 3902 CA CYS B 285 23.367 −8.177 2.783 1.00 33.98 C ATOM 3903 C CYS B 285 23.963 −6.788 2.975 1.00 37.16 C ATOM 3904 O CYS B 285 24.749 −6.339 2.141 1.00 41.34 O ATOM 3905 CB CYS B 285 22.173 −8.080 1.833 1.00 37.08 C ATOM 3906 SG CYS B 285 21.591 −9.662 1.189 1.00 50.19 S ATOM 3907 N TRP B 286 23.595 −6.105 4.055 1.00 31.92 N ATOM 3908 CA TRP B 286 24.061 −4.735 4.265 1.00 29.35 C ATOM 3909 C TRP B 286 25.088 −4.569 5.368 1.00 32.19 C ATOM 3910 O TRP B 286 25.784 −3.562 5.423 1.00 34.52 O ATOM 3911 CB TRP B 286 22.890 −3.806 4.557 1.00 31.50 C ATOM 3912 CG TRP B 286 22.254 −3.276 3.344 1.00 25.60 C ATOM 3913 CD1 TRP B 286 20.997 −3.537 2.909 1.00 27.81 C ATOM 3914 CD2 TRP B 286 22.841 −2.389 2.386 1.00 28.95 C ATOM 3915 NE1 TRP B 286 20.752 −2.863 1.747 1.00 30.10 N ATOM 3916 CE2 TRP B 286 21.870 −2.151 1.396 1.00 28.81 C ATOM 3917 CE3 TRP B 286 24.092 −1.771 2.269 1.00 31.32 C ATOM 3918 CZ2 TRP B 286 22.109 −1.318 0.291 1.00 23.35 C ATOM 3919 CZ3 TRP B 286 24.330 −0.946 1.167 1.00 29.28 C ATOM 3920 CH2 TRP B 286 23.342 −0.731 0.196 1.00 25.66 C ATOM 3921 N LEU B 287 25.180 −5.540 6.261 1.00 32.90 N ATOM 3922 CA LEU B 287 26.043 −5.358 7.413 1.00 36.95 C ATOM 3923 C LEU B 287 27.519 −5.306 7.031 1.00 40.58 C ATOM 3924 O LEU B 287 28.247 −4.433 7.505 1.00 45.74 O ATOM 3925 CB LEU B 287 25.769 −6.397 8.502 1.00 33.98 C ATOM 3926 CG LEU B 287 26.406 −6.076 9.858 1.00 49.15 C ATOM 3927 CD1 LEU B 287 26.106 −4.636 10.309 1.00 39.22 C ATOM 3928 CD2 LEU B 287 25.959 −7.090 10.898 1.00 41.08 C ATOM 3929 N PRO B 288 27.973 −6.230 6.171 1.00 43.68 N ATOM 3930 CA PRO B 288 29.393 −6.165 5.796 1.00 47.21 C ATOM 3931 C PRO B 288 29.804 −4.751 5.396 1.00 40.01 C ATOM 3932 O PRO B 288 30.824 −4.241 5.866 1.00 35.77 O ATOM 3933 CB PRO B 288 29.482 −7.119 4.604 1.00 32.14 C ATOM 3934 CG PRO B 288 28.423 −8.133 4.884 1.00 38.96 C ATOM 3935 CD PRO B 288 27.297 −7.394 5.571 1.00 37.58 C ATOM 3936 N PHE B 289 28.997 −4.123 4.550 1.00 37.73 N ATOM 3937 CA PHE B 289 29.286 −2.774 4.077 1.00 38.25 C ATOM 3938 C PHE B 289 29.400 −1.747 5.217 1.00 40.34 C ATOM 3939 O PHE B 289 30.352 −0.966 5.258 1.00 39.60 O ATOM 3940 CB PHE B 289 28.233 −2.332 3.055 1.00 31.65 C ATOM 3941 CG PHE B 289 28.362 −0.899 2.635 1.00 31.12 C ATOM 3942 CD1 PHE B 289 29.163 −0.553 1.555 1.00 29.50 C ATOM 3943 CD2 PHE B 289 27.678 0.108 3.318 1.00 30.72 C ATOM 3944 CE1 PHE B 289 29.286 0.771 1.158 1.00 27.39 C ATOM 3945 CE2 PHE B 289 27.792 1.428 2.925 1.00 29.10 C ATOM 3946 CZ PHE B 289 28.604 1.760 1.837 1.00 27.98 C ATOM 3947 N PHE B 290 28.445 −1.747 6.143 1.00 32.33 N ATOM 3948 CA PHE B 290 28.497 −0.796 7.256 1.00 38.30 C ATOM 3949 C PHE B 290 29.599 −1.095 8.265 1.00 40.74 C ATOM 3950 O PHE B 290 30.138 −0.175 8.887 1.00 40.50 O ATOM 3951 CB PHE B 290 27.134 −0.629 7.933 1.00 29.59 C ATOM 3952 CG PHE B 290 26.176 0.148 7.105 1.00 28.76 C ATOM 3953 CD1 PHE B 290 25.183 −0.492 6.385 1.00 27.65 C ATOM 3954 CD2 PHE B 290 26.308 1.522 6.989 1.00 30.86 C ATOM 3955 CE1 PHE B 290 24.315 0.233 5.585 1.00 28.34 C ATOM 3956 CE2 PHE B 290 25.448 2.258 6.184 1.00 26.31 C ATOM 3957 CZ PHE B 290 24.450 1.614 5.486 1.00 26.58 C ATOM 3958 N LEU B 291 29.937 −2.372 8.425 1.00 34.81 N ATOM 3959 CA LEU B 291 31.112 −2.733 9.202 1.00 38.20 C ATOM 3960 C LEU B 291 32.345 −2.115 8.552 1.00 43.44 C ATOM 3961 O LEU B 291 33.100 −1.385 9.198 1.00 37.62 O ATOM 3962 CB LEU B 291 31.283 −4.252 9.289 1.00 44.87 C ATOM 3963 CG LEU B 291 30.333 −5.010 10.213 1.00 55.65 C ATOM 3964 CD1 LEU B 291 31.004 −6.290 10.685 1.00 46.10 C ATOM 3965 CD2 LEU B 291 29.941 −4.149 11.397 1.00 34.59 C ATOM 3966 N VAL B 292 32.534 −2.404 7.267 1.00 38.80 N ATOM 3967 CA VAL B 292 33.696 −1.914 6.536 1.00 46.04 C ATOM 3968 C VAL B 292 33.750 −0.390 6.562 1.00 46.24 C ATOM 3969 O VAL B 292 34.823 0.213 6.568 1.00 48.97 O ATOM 3970 CB VAL B 292 33.714 −2.435 5.083 1.00 43.91 C ATOM 3971 CG1 VAL B 292 34.564 −1.544 4.204 1.00 54.22 C ATOM 3972 CG2 VAL B 292 34.233 −3.850 5.048 1.00 44.98 C ATOM 3973 N ASN B 293 32.578 0.226 6.594 1.00 45.15 N ATOM 3974 CA ASN B 293 32.479 1.671 6.621 1.00 49.65 C ATOM 3975 C ASN B 293 33.119 2.268 7.871 1.00 49.84 C ATOM 3976 O ASN B 293 33.792 3.301 7.811 1.00 51.95 O ATOM 3977 CB ASN B 293 31.013 2.085 6.536 1.00 46.41 C ATOM 3978 CG ASN B 293 30.832 3.430 5.881 1.00 50.98 C ATOM 3979 OD1 ASN B 293 31.401 3.699 4.823 1.00 49.29 O ATOM 3980 ND2 ASN B 293 30.040 4.289 6.508 1.00 52.67 N ATOM 3981 N ILE B 294 32.908 1.618 9.008 1.00 50.69 N ATOM 3982 CA ILE B 294 33.437 2.133 10.264 1.00 48.46 C ATOM 3983 C ILE B 294 34.924 1.836 10.430 1.00 41.51 C ATOM 3984 O ILE B 294 35.703 2.734 10.744 1.00 33.86 O ATOM 3985 CB ILE B 294 32.664 1.592 11.451 1.00 44.57 C ATOM 3986 CG1 ILE B 294 31.196 1.994 11.332 1.00 43.04 C ATOM 3987 CG2 ILE B 294 33.254 2.135 12.740 1.00 61.37 C ATOM 3988 CD1 ILE B 294 30.296 1.183 12.221 1.00 51.39 C ATOM 3989 N VAL B 295 35.307 0.579 10.208 1.00 43.66 N ATOM 3990 CA VAL B 295 36.713 0.190 10.199 1.00 38.22 C ATOM 3991 C VAL B 295 37.551 1.227 9.465 1.00 41.50 C ATOM 3992 O VAL B 295 38.590 1.653 9.957 1.00 45.20 O ATOM 3993 CB VAL B 295 36.934 −1.177 9.526 1.00 32.19 C ATOM 3994 CG1 VAL B 295 38.398 −1.345 9.162 1.00 40.23 C ATOM 3995 CG2 VAL B 295 36.494 −2.301 10.439 1.00 22.56 C ATOM 3996 N ASN B 296 37.087 1.631 8.289 1.00 38.25 N ATOM 3997 CA ASN B 296 37.775 2.646 7.494 1.00 50.48 C ATOM 3998 C ASN B 296 38.030 3.959 8.224 1.00 52.00 C ATOM 3999 O ASN B 296 39.084 4.579 8.057 1.00 56.60 O ATOM 4000 CB ASN B 296 37.008 2.929 6.199 1.00 53.54 C ATOM 4001 CG ASN B 296 37.769 2.503 4.965 1.00 64.71 C ATOM 4002 OD1 ASN B 296 38.916 2.055 5.046 1.00 69.84 O ATOM 4003 ND2 ASN B 296 37.137 2.649 3.808 1.00 83.43 N ATOM 4004 N VAL B 297 37.054 4.396 9.012 1.00 54.20 N ATOM 4005 CA VAL B 297 37.185 5.646 9.748 1.00 57.14 C ATOM 4006 C VAL B 297 38.416 5.595 10.652 1.00 60.38 C ATOM 4007 O VAL B 297 39.130 6.584 10.803 1.00 52.82 O ATOM 4008 CB VAL B 297 35.923 5.940 10.577 1.00 41.85 C ATOM 4009 CG1 VAL B 297 36.091 7.219 11.368 1.00 41.12 C ATOM 4010 CG2 VAL B 297 34.721 6.036 9.663 1.00 50.01 C ATOM 4011 N PHE B 298 38.667 4.424 11.229 1.00 55.55 N ATOM 4012 CA PHE B 298 39.784 4.223 12.145 1.00 61.29 C ATOM 4013 C PHE B 298 41.107 4.092 11.399 1.00 64.30 C ATOM 4014 O PHE B 298 42.107 4.701 11.772 1.00 73.40 O ATOM 4015 CB PHE B 298 39.539 2.969 12.984 1.00 56.63 C ATOM 4016 CG PHE B 298 38.412 3.108 13.959 1.00 61.48 C ATOM 4017 CD1 PHE B 298 37.555 4.200 13.901 1.00 74.29 C ATOM 4018 CD2 PHE B 298 38.191 2.139 14.922 1.00 85.08 C ATOM 4019 CE1 PHE B 298 36.509 4.335 14.796 1.00 69.53 C ATOM 4020 CE2 PHE B 298 37.144 2.264 15.822 1.00 97.65 C ATOM 4021 CZ PHE B 298 36.302 3.365 15.758 1.00 84.42 C ATOM 4022 N ASN B 299 41.093 3.304 10.331 1.00 66.84 N ATOM 4023 CA ASN B 299 42.306 2.965 9.609 1.00 66.63 C ATOM 4024 C ASN B 299 42.070 2.816 8.114 1.00 76.14 C ATOM 4025 O ASN B 299 41.901 1.696 7.629 1.00 75.50 O ATOM 4026 CB ASN B 299 42.858 1.650 10.155 1.00 76.75 C ATOM 4027 CG ASN B 299 44.130 1.227 9.469 1.00 69.48 C ATOM 4028 OD1 ASN B 299 44.817 2.038 8.854 1.00 72.96 O ATOM 4029 ND2 ASN B 299 44.459 −0.051 9.580 1.00 75.80 N ATOM 4030 N ARG B 300 42.050 3.937 7.388 1.00 93.03 N ATOM 4031 CA ARG B 300 41.973 3.901 5.926 1.00 73.87 C ATOM 4032 C ARG B 300 43.115 3.017 5.456 1.00 79.24 C ATOM 4033 O ARG B 300 44.187 3.034 6.057 1.00 99.16 O ATOM 4034 CB ARG B 300 42.108 5.307 5.311 1.00 66.81 C ATOM 4035 CG ARG B 300 41.261 6.398 5.987 1.00 94.31 C ATOM 4036 CD ARG B 300 40.857 7.526 5.020 1.00 104.58 C ATOM 4037 NE ARG B 300 40.058 8.574 5.669 1.00 112.59 N ATOM 4038 CZ ARG B 300 39.306 9.468 5.025 1.00 109.58 C ATOM 4039 NH1 ARG B 300 39.228 9.452 3.700 1.00 90.81 N ATOM 4040 NH2 ARG B 300 38.623 10.380 5.706 1.00 100.99 N ATOM 4041 N ASP B 301 42.885 2.226 4.413 1.00 79.25 N ATOM 4042 CA ASP B 301 43.936 1.381 3.832 1.00 89.04 C ATOM 4043 C ASP B 301 44.203 0.082 4.595 1.00 82.82 C ATOM 4044 O ASP B 301 45.295 −0.473 4.506 1.00 87.79 O ATOM 4045 CB ASP B 301 45.261 2.147 3.687 1.00 84.04 C ATOM 4046 CG ASP B 301 45.085 3.525 3.074 1.00 104.08 C ATOM 4047 OD1 ASP B 301 44.131 3.717 2.286 1.00 107.47 O ATOM 4048 OD2 ASP B 301 45.915 4.413 3.382 1.00 97.26 O ATOM 4049 N LEU B 302 43.224 −0.397 5.349 1.00 75.64 N ATOM 4050 CA LEU B 302 43.331 −1.725 5.943 1.00 74.99 C ATOM 4051 C LEU B 302 42.476 −2.724 5.169 1.00 91.10 C ATOM 4052 O LEU B 302 42.692 −3.937 5.244 1.00 92.93 O ATOM 4053 CB LEU B 302 42.884 −1.723 7.395 1.00 76.08 C ATOM 4054 CG LEU B 302 42.825 −3.163 7.901 1.00 72.25 C ATOM 4055 CD1 LEU B 302 44.237 −3.644 8.209 1.00 81.61 C ATOM 4056 CD2 LEU B 302 41.913 −3.306 9.104 1.00 72.79 C ATOM 4057 N VAL B 303 41.490 −2.208 4.441 1.00 85.48 N ATOM 4058 CA VAL B 303 40.637 −3.035 3.595 1.00 62.71 C ATOM 4059 C VAL B 303 40.501 −2.407 2.206 1.00 69.04 C ATOM 4060 O VAL B 303 40.294 −1.196 2.079 1.00 69.37 O ATOM 4061 CB VAL B 303 39.263 −3.289 4.253 1.00 75.11 C ATOM 4062 CG1 VAL B 303 38.226 −3.700 3.219 1.00 65.87 C ATOM 4063 CG2 VAL B 303 39.395 −4.353 5.341 1.00 77.22 C ATOM 4064 N PRO B 304 40.644 −3.237 1.160 1.00 61.83 N ATOM 4065 CA PRO B 304 40.801 −2.843 −0.248 1.00 48.47 C ATOM 4066 C PRO B 304 39.559 −2.252 −0.917 1.00 50.91 C ATOM 4067 O PRO B 304 38.502 −2.882 −0.931 1.00 48.78 O ATOM 4068 CB PRO B 304 41.170 −4.166 −0.923 1.00 45.74 C ATOM 4069 CG PRO B 304 40.549 −5.195 −0.039 1.00 47.82 C ATOM 4070 CD PRO B 304 40.838 −4.687 1.327 1.00 54.22 C ATOM 4071 N ASP B 305 39.718 −1.060 −1.490 1.00 54.04 N ATOM 4072 CA ASP B 305 38.667 −0.353 −2.229 1.00 58.93 C ATOM 4073 C ASP B 305 37.717 −1.255 −3.019 1.00 56.48 C ATOM 4074 O ASP B 305 36.516 −0.995 −3.098 1.00 51.52 O ATOM 4075 CB ASP B 305 39.293 0.657 −3.202 1.00 70.59 C ATOM 4076 CG ASP B 305 39.599 2.002 −2.554 1.00 96.69 C ATOM 4077 OD1 ASP B 305 38.853 2.427 −1.646 1.00 97.96 O ATOM 4078 OD2 ASP B 305 40.584 2.649 −2.974 1.00 108.96 O ATOM 4079 N TRP B 306 38.258 −2.298 −3.633 1.00 55.67 N ATOM 4080 CA TRP B 306 37.458 −3.149 −4.504 1.00 53.47 C ATOM 4081 C TRP B 306 36.477 −4.002 −3.706 1.00 48.21 C ATOM 4082 O TRP B 306 35.399 −4.331 −4.199 1.00 50.15 O ATOM 4083 CB TRP B 306 38.356 −4.028 −5.376 1.00 47.81 C ATOM 4084 CG TRP B 306 39.122 −5.025 −4.597 1.00 49.03 C ATOM 4085 CD1 TRP B 306 40.417 −4.922 −4.176 1.00 52.58 C ATOM 4086 CD2 TRP B 306 38.644 −6.289 −4.127 1.00 47.34 C ATOM 4087 NE1 TRP B 306 40.776 −6.050 −3.474 1.00 55.27 N ATOM 4088 CE2 TRP B 306 39.706 −6.904 −3.427 1.00 50.01 C ATOM 4089 CE3 TRP B 306 37.420 −6.958 −4.221 1.00 44.70 C ATOM 4090 CZ2 TRP B 306 39.581 −8.154 −2.828 1.00 44.01 C ATOM 4091 CZ3 TRP B 306 37.299 −8.202 −3.626 1.00 56.92 C ATOM 4092 CH2 TRP B 306 38.374 −8.787 −2.939 1.00 51.66 C ATOM 4093 N LEU B 307 36.855 −4.350 −2.477 1.00 41.26 N ATOM 4094 CA LEU B 307 35.996 −5.115 −1.582 1.00 41.97 C ATOM 4095 C LEU B 307 34.963 −4.184 −0.968 1.00 42.23 C ATOM 4096 O LEU B 307 33.851 −4.584 −0.619 1.00 34.18 O ATOM 4097 CB LEU B 307 36.624 −5.763 −0.480 1.00 48.22 C ATOM 4098 CG LEU B 307 36.036 −6.521 0.587 1.00 49.79 C ATOM 4099 CD1 LEU B 307 35.234 −7.660 −0.026 1.00 43.18 C ATOM 4100 CD2 LEU B 307 36.973 −7.037 1.662 1.00 50.14 C ATOM 4101 N PHE B 308 35.351 −2.926 −0.834 1.00 43.47 N ATOM 4102 CA PHE B 308 34.411 −1.892 −0.469 1.00 41.35 C ATOM 4103 C PHE B 308 33.278 −1.947 −1.488 1.00 38.66 C ATOM 4104 O PHE B 308 32.113 −2.094 −1.127 1.00 42.40 O ATOM 4105 CB PHE B 308 35.114 −0.536 −0.496 1.00 50.21 C ATOM 4106 CG PHE B 308 34.470 0.501 0.370 1.00 59.59 C ATOM 4107 CD1 PHE B 308 34.804 0.605 1.707 1.00 60.05 C ATOM 4108 CD2 PHE B 308 33.534 1.380 −0.156 1.00 75.99 C ATOM 4109 CE1 PHE B 308 34.208 1.556 2.512 1.00 68.58 C ATOM 4110 CE2 PHE B 308 32.935 2.342 0.644 1.00 74.46 C ATOM 4111 CZ PHE B 308 33.270 2.427 1.981 1.00 65.90 C ATOM 4112 N VAL B 309 33.631 −1.863 −2.768 1.00 45.30 N ATOM 4113 CA VAL B 309 32.645 −1.896 −3.847 1.00 46.64 C ATOM 4114 C VAL B 309 31.856 −3.212 −3.895 1.00 43.26 C ATOM 4115 O VAL B 309 30.623 −3.196 −4.017 1.00 32.66 O ATOM 4116 CB VAL B 309 33.300 −1.593 −5.213 1.00 46.44 C ATOM 4117 CG1 VAL B 309 32.341 −1.900 −6.350 1.00 46.73 C ATOM 4118 CG2 VAL B 309 33.740 −0.142 −5.271 1.00 32.25 C ATOM 4119 N ALA B 310 32.567 −4.337 −3.795 1.00 39.44 N ATOM 4120 CA ALA B 310 31.939 −5.658 −3.717 1.00 35.64 C ATOM 4121 C ALA B 310 30.790 −5.686 −2.716 1.00 38.80 C ATOM 4122 O ALA B 310 29.682 −6.107 −3.044 1.00 30.02 O ATOM 4123 CB ALA B 310 32.959 −6.708 −3.340 1.00 31.85 C ATOM 4124 N PHE B 311 31.067 −5.237 −1.492 1.00 38.34 N ATOM 4125 CA PHE B 311 30.077 −5.239 −0.419 1.00 28.59 C ATOM 4126 C PHE B 311 28.886 −4.312 −0.679 1.00 29.02 C ATOM 4127 O PHE B 311 27.755 −4.630 −0.322 1.00 29.45 O ATOM 4128 CB PHE B 311 30.734 −4.919 0.932 1.00 28.99 C ATOM 4129 CG PHE B 311 31.404 −6.101 1.580 1.00 33.91 C ATOM 4130 CD1 PHE B 311 32.492 −5.928 2.426 1.00 34.82 C ATOM 4131 CD2 PHE B 311 30.955 −7.392 1.329 1.00 33.09 C ATOM 4132 CE1 PHE B 311 33.115 −7.022 3.023 1.00 40.11 C ATOM 4133 CE2 PHE B 311 31.570 −8.494 1.918 1.00 37.41 C ATOM 4134 CZ PHE B 311 32.653 −8.309 2.769 1.00 42.16 C ATOM 4135 N ASN B 312 29.130 −3.168 −1.299 1.00 27.12 N ATOM 4136 CA ASN B 312 28.037 −2.258 −1.599 1.00 29.15 C ATOM 4137 C ASN B 312 27.079 −2.866 −2.644 1.00 30.87 C ATOM 4138 O ASN B 312 25.873 −2.612 −2.625 1.00 27.51 O ATOM 4139 CB ASN B 312 28.598 −0.903 −2.046 1.00 27.89 C ATOM 4140 CG ASN B 312 27.550 0.207 −2.072 1.00 30.52 C ATOM 4141 OD1 ASN B 312 27.881 1.375 −2.277 1.00 28.28 O ATOM 4142 ND2 ASN B 312 26.285 −0.153 −1.879 1.00 38.95 N ATOM 4143 N TRP B 313 27.617 −3.679 −3.549 1.00 33.37 N ATOM 4144 CA TRP B 313 26.793 −4.376 −4.545 1.00 30.63 C ATOM 4145 C TRP B 313 26.006 −5.539 −3.939 1.00 28.36 C ATOM 4146 O TRP B 313 24.968 −5.951 −4.471 1.00 22.30 O ATOM 4147 CB TRP B 313 27.634 −4.826 −5.755 1.00 25.72 C ATOM 4148 CG TRP B 313 27.804 −3.719 −6.725 1.00 27.45 C ATOM 4149 CD1 TRP B 313 28.788 −2.778 −6.733 1.00 30.63 C ATOM 4150 CD2 TRP B 313 26.925 −3.387 −7.804 1.00 32.67 C ATOM 4151 NE1 TRP B 313 28.589 −1.887 −7.762 1.00 29.11 N ATOM 4152 CE2 TRP B 313 27.447 −2.239 −8.433 1.00 35.63 C ATOM 4153 CE3 TRP B 313 25.745 −3.945 −8.296 1.00 24.71 C ATOM 4154 CZ2 TRP B 313 26.832 −1.648 −9.529 1.00 31.43 C ATOM 4155 CZ3 TRP B 313 25.144 −3.355 −9.377 1.00 30.25 C ATOM 4156 CH2 TRP B 313 25.688 −2.220 −9.984 1.00 32.80 C ATOM 4157 N LEU B 314 26.507 −6.057 −2.821 1.00 25.74 N ATOM 4158 CA LEU B 314 25.784 −7.054 −2.063 1.00 25.68 C ATOM 4159 C LEU B 314 24.577 −6.377 −1.415 1.00 31.54 C ATOM 4160 O LEU B 314 23.503 −6.958 −1.306 1.00 32.21 O ATOM 4161 CB LEU B 314 26.686 −7.688 −1.014 1.00 20.61 C ATOM 4162 CG LEU B 314 25.933 −8.727 −0.181 1.00 25.27 C ATOM 4163 CD1 LEU B 314 25.356 −9.809 −1.075 1.00 25.89 C ATOM 4164 CD2 LEU B 314 26.843 −9.333 0.854 1.00 29.10 C ATOM 4165 N GLY B 315 24.754 −5.129 −1.003 1.00 30.86 N ATOM 4166 CA GLY B 315 23.643 −4.358 −0.489 1.00 27.54 C ATOM 4167 C GLY B 315 22.620 −4.077 −1.574 1.00 28.89 C ATOM 4168 O GLY B 315 21.409 −4.152 −1.335 1.00 28.05 O ATOM 4169 N TYR B 316 23.106 −3.733 −2.765 1.00 24.69 N ATOM 4170 CA TYR B 316 22.218 −3.440 −3.881 1.00 32.67 C ATOM 4171 C TYR B 316 21.396 −4.660 −4.284 1.00 35.98 C ATOM 4172 O TYR B 316 20.224 −4.536 −4.626 1.00 36.28 O ATOM 4173 CB TYR B 316 23.002 −2.971 −5.098 1.00 37.19 C ATOM 4174 CG TYR B 316 23.545 −1.566 −5.019 1.00 39.21 C ATOM 4175 CD1 TYR B 316 24.654 −1.196 −5.776 1.00 34.11 C ATOM 4176 CD2 TYR B 316 22.958 −0.610 −4.205 1.00 31.57 C ATOM 4177 CE1 TYR B 316 25.159 0.075 −5.724 1.00 33.52 C ATOM 4178 CE2 TYR B 316 23.469 0.678 −4.145 1.00 33.06 C ATOM 4179 CZ TYR B 316 24.568 1.007 −4.907 1.00 35.13 C ATOM 4180 OH TYR B 316 25.099 2.265 −4.865 1.00 36.76 O ATOM 4181 N ALA B 317 22.028 −5.832 −4.265 1.00 42.14 N ATOM 4182 CA ALA B 317 21.381 −7.078 −4.683 1.00 42.55 C ATOM 4183 C ALA B 317 20.210 −7.458 −3.773 1.00 41.00 C ATOM 4184 O ALA B 317 19.226 −8.054 −4.219 1.00 44.32 O ATOM 4185 CB ALA B 317 22.400 −8.215 −4.755 1.00 27.04 C ATOM 4186 N ASN B 318 20.321 −7.121 −2.495 1.00 30.05 N ATOM 4187 CA ASN B 318 19.213 −7.312 −1.591 1.00 37.27 C ATOM 4188 C ASN B 318 17.892 −6.907 −2.260 1.00 33.39 C ATOM 4189 O ASN B 318 16.883 −7.582 −2.107 1.00 42.69 O ATOM 4190 CB ASN B 318 19.437 −6.497 −0.314 1.00 47.49 C ATOM 4191 CG ASN B 318 18.362 −6.737 0.732 1.00 44.43 C ATOM 4192 OD1 ASN B 318 18.403 −7.735 1.461 1.00 39.86 O ATOM 4193 ND2 ASN B 318 17.392 −5.820 0.811 1.00 31.10 N ATOM 4194 N SER B 319 17.908 −5.818 −3.015 1.00 25.28 N ATOM 4195 CA SER B 319 16.691 −5.290 −3.624 1.00 31.76 C ATOM 4196 C SER B 319 15.993 −6.272 −4.551 1.00 39.75 C ATOM 4197 O SER B 319 14.843 −6.062 −4.932 1.00 41.67 O ATOM 4198 CB SER B 319 16.972 −4.000 −4.392 1.00 32.97 C ATOM 4199 OG SER B 319 17.169 −2.914 −3.512 1.00 37.26 O ATOM 4200 N ALA B 320 16.681 −7.345 −4.917 1.00 41.37 N ATOM 4201 CA ALA B 320 16.077 −8.350 −5.775 1.00 38.02 C ATOM 4202 C ALA B 320 15.660 −9.606 −5.000 1.00 43.74 C ATOM 4203 O ALA B 320 14.931 −10.455 −5.511 1.00 45.02 O ATOM 4204 CB ALA B 320 17.011 −8.697 −6.903 1.00 33.95 C ATOM 4205 N MET B 321 16.107 −9.715 −3.756 1.00 39.48 N ATOM 4206 CA MET B 321 15.824 −10.903 −2.962 1.00 49.18 C ATOM 4207 C MET B 321 14.395 −10.983 −2.412 1.00 45.35 C ATOM 4208 O MET B 321 13.853 −12.074 −2.234 1.00 45.04 O ATOM 4209 CB MET B 321 16.861 −11.050 −1.848 1.00 43.74 C ATOM 4210 CG MET B 321 18.238 −11.338 −2.411 1.00 48.21 C ATOM 4211 SD MET B 321 19.583 −11.142 −1.248 1.00 58.51 S ATOM 4212 CE MET B 321 21.010 −11.259 −2.335 1.00 40.14 C ATOM 4213 N ASN B 322 13.785 −9.834 −2.160 1.00 47.80 N ATOM 4214 CA ASN B 322 12.442 −9.802 −1.586 1.00 53.01 C ATOM 4215 C ASN B 322 11.396 −10.563 −2.386 1.00 52.55 C ATOM 4216 O ASN B 322 10.763 −11.479 −1.858 1.00 49.35 O ATOM 4217 CB ASN B 322 11.969 −8.363 −1.372 1.00 56.63 C ATOM 4218 CG ASN B 322 12.400 −7.813 −0.052 1.00 56.12 C ATOM 4219 OD1 ASN B 322 13.196 −8.433 0.656 1.00 37.66 O ATOM 4220 ND2 ASN B 322 11.877 −6.644 0.301 1.00 59.29 N ATOM 4221 N PRO B 323 11.187 −10.169 −3.655 1.00 52.48 N ATOM 4222 CA PRO B 323 10.149 −10.855 −4.427 1.00 54.93 C ATOM 4223 C PRO B 323 10.424 −12.353 −4.480 1.00 48.25 C ATOM 4224 O PRO B 323 9.485 −13.137 −4.384 1.00 49.60 O ATOM 4225 CB PRO B 323 10.262 −10.213 −5.812 1.00 43.24 C ATOM 4226 CG PRO B 323 10.826 −8.865 −5.542 1.00 43.18 C ATOM 4227 CD PRO B 323 11.812 −9.086 −4.433 1.00 47.45 C ATOM 4228 N ILE B 324 11.689 −12.740 −4.602 1.00 40.45 N ATOM 4229 CA ILE B 324 12.053 −14.150 −4.534 1.00 50.35 C ATOM 4230 C ILE B 324 11.576 −14.799 −3.236 1.00 55.01 C ATOM 4231 O ILE B 324 10.930 −15.844 −3.260 1.00 54.80 O ATOM 4232 CB ILE B 324 13.569 −14.357 −4.641 1.00 54.63 C ATOM 4233 CG1 ILE B 324 14.014 −14.268 −6.102 1.00 58.01 C ATOM 4234 CG2 ILE B 324 13.968 −15.705 −4.024 1.00 38.15 C ATOM 4235 CD1 ILE B 324 15.504 −14.032 −6.266 1.00 59.49 C ATOM 4236 N ILE B 325 11.900 −14.180 −2.104 1.00 50.59 N ATOM 4237 CA ILE B 325 11.526 −14.727 −0.809 1.00 45.25 C ATOM 4238 C ILE B 325 10.009 −14.859 −0.662 1.00 54.51 C ATOM 4239 O ILE B 325 9.513 −15.822 −0.083 1.00 47.16 O ATOM 4240 CB ILE B 325 12.089 −13.877 0.344 1.00 47.93 C ATOM 4241 CG1 ILE B 325 13.610 −13.810 0.261 1.00 44.81 C ATOM 4242 CG2 ILE B 325 11.672 −14.448 1.698 1.00 50.75 C ATOM 4243 CD1 ILE B 325 14.263 −13.276 1.518 1.00 43.70 C ATOM 4244 N TYR B 326 9.271 −13.891 −1.192 1.00 59.16 N ATOM 4245 CA TYR B 326 7.816 −13.928 −1.097 1.00 62.17 C ATOM 4246 C TYR B 326 7.226 −15.174 −1.764 1.00 65.37 C ATOM 4247 O TYR B 326 6.065 −15.509 −1.542 1.00 62.21 O ATOM 4248 CB TYR B 326 7.190 −12.666 −1.690 1.00 50.49 C ATOM 4249 CG TYR B 326 7.516 −11.404 −0.933 1.00 57.04 C ATOM 4250 CD1 TYR B 326 7.624 −10.187 −1.596 1.00 56.32 C ATOM 4251 CD2 TYR B 326 7.724 −11.426 0.448 1.00 54.66 C ATOM 4252 CE1 TYR B 326 7.918 −9.026 −0.911 1.00 55.62 C ATOM 4253 CE2 TYR B 326 8.024 −10.265 1.145 1.00 48.65 C ATOM 4254 CZ TYR B 326 8.120 −9.067 0.456 1.00 50.63 C ATOM 4255 OH TYR B 326 8.418 −7.899 1.117 1.00 41.84 O ATOM 4256 N CYS B 327 8.029 −15.856 −2.575 1.00 65.19 N ATOM 4257 CA CYS B 327 7.586 −17.076 −3.252 1.00 72.20 C ATOM 4258 C CYS B 327 7.301 −18.219 −2.277 1.00 75.01 C ATOM 4259 O CYS B 327 6.910 −19.311 −2.687 1.00 79.31 O ATOM 4260 CB CYS B 327 8.622 −17.534 −4.282 1.00 61.73 C ATOM 4261 SG CYS B 327 8.802 −16.431 −5.685 1.00 66.78 S ATOM 4262 N ARG B 328 7.508 −17.974 −0.990 1.00 63.43 N ATOM 4263 CA ARG B 328 7.196 −18.974 0.017 1.00 68.93 C ATOM 4264 C ARG B 328 5.692 −19.105 0.186 1.00 79.34 C ATOM 4265 O ARG B 328 5.181 −20.189 0.463 1.00 95.48 O ATOM 4266 CB ARG B 328 7.830 −18.602 1.355 1.00 73.91 C ATOM 4267 CG ARG B 328 9.285 −19.011 1.502 1.00 70.97 C ATOM 4268 CD ARG B 328 9.850 −18.392 2.751 1.00 61.12 C ATOM 4269 NE ARG B 328 8.818 −18.286 3.781 1.00 64.50 N ATOM 4270 CZ ARG B 328 8.745 −19.071 4.852 1.00 76.70 C ATOM 4271 NH1 ARG B 328 9.655 −20.021 5.044 1.00 78.29 N ATOM 4272 NH2 ARG B 328 7.768 −18.902 5.735 1.00 74.08 N ATOM 4273 N SER B 329 4.987 −17.994 0.013 1.00 85.09 N ATOM 4274 CA SER B 329 3.549 −17.959 0.234 1.00 90.96 C ATOM 4275 C SER B 329 2.783 −18.606 −0.905 1.00 91.66 C ATOM 4276 O SER B 329 3.144 −18.454 −2.075 1.00 75.69 O ATOM 4277 CB SER B 329 3.061 −16.520 0.439 1.00 95.01 C ATOM 4278 OG SER B 329 1.672 −16.480 0.728 1.00 87.75 O ATOM 4279 N PRO B 330 1.735 −19.357 −0.539 1.00 110.04 N ATOM 4280 CA PRO B 330 0.666 −19.836 −1.417 1.00 110.61 C ATOM 4281 C PRO B 330 −0.020 −18.641 −2.075 1.00 112.13 C ATOM 4282 O PRO B 330 −0.065 −18.560 −3.304 1.00 104.27 O ATOM 4283 CB PRO B 330 −0.295 −20.527 −0.444 1.00 111.18 C ATOM 4284 CG PRO B 330 0.562 −20.937 0.710 1.00 102.08 C ATOM 4285 CD PRO B 330 1.591 −19.859 0.841 1.00 101.96 C ATOM 4286 N ASP B 331 −0.537 −17.728 −1.251 1.00 111.51 N ATOM 4287 CA ASP B 331 −1.109 −16.467 −1.721 1.00 110.54 C ATOM 4288 C ASP B 331 −0.257 −15.790 −2.785 1.00 113.28 C ATOM 4289 O ASP B 331 −0.674 −15.665 −3.938 1.00 114.79 O ATOM 4290 CB ASP B 331 −1.312 −15.499 −0.553 1.00 112.25 C ATOM 4291 CG ASP B 331 −2.771 −15.246 −0.259 1.00 127.64 C ATOM 4292 OD1 ASP B 331 −3.620 −15.882 −0.915 1.00 135.05 O ATOM 4293 OD2 ASP B 331 −3.069 −14.406 0.617 1.00 137.73 O ATOM 4294 N PHE B 332 0.932 −15.343 −2.392 1.00 111.66 N ATOM 4295 CA PHE B 332 1.837 −14.685 −3.328 1.00 108.21 C ATOM 4296 C PHE B 332 2.209 −15.598 −4.505 1.00 111.38 C ATOM 4297 O PHE B 332 2.522 −15.119 −5.594 1.00 109.32 O ATOM 4298 CB PHE B 332 3.091 −14.168 −2.610 1.00 101.50 C ATOM 4299 CG PHE B 332 2.887 −12.860 −1.877 1.00 94.15 C ATOM 4300 CD1 PHE B 332 3.517 −12.624 −0.658 1.00 89.30 C ATOM 4301 CD2 PHE B 332 2.068 −11.871 −2.407 1.00 75.63 C ATOM 4302 CE1 PHE B 332 3.341 −11.425 0.017 1.00 65.14 C ATOM 4303 CE2 PHE B 332 1.887 −10.675 −1.742 1.00 77.85 C ATOM 4304 CZ PHE B 332 2.525 −10.451 −0.527 1.00 86.15 C ATOM 4305 N ARG B 333 2.157 −16.910 −4.289 1.00 110.44 N ATOM 4306 CA ARG B 333 2.428 −17.867 −5.358 1.00 107.49 C ATOM 4307 C ARG B 333 1.306 −17.862 −6.398 1.00 102.94 C ATOM 4308 O ARG B 333 1.567 −17.856 −7.598 1.00 106.52 O ATOM 4309 CB ARG B 333 2.610 −19.270 −4.781 1.00 100.76 C ATOM 4310 CG ARG B 333 3.538 −20.171 −5.579 1.00 100.36 C ATOM 4311 CD ARG B 333 4.131 −21.228 −4.668 1.00 90.01 C ATOM 4312 NE ARG B 333 3.176 −21.620 −3.635 1.00 99.45 N ATOM 4313 CZ ARG B 333 3.509 −21.949 −2.391 1.00 101.47 C ATOM 4314 NH1 ARG B 333 4.783 −21.931 −2.015 1.00 86.95 N ATOM 4315 NH2 ARG B 333 2.568 −22.288 −1.517 1.00 88.95 N ATOM 4316 N LYS B 334 0.061 −17.853 −5.931 1.00 99.16 N ATOM 4317 CA LYS B 334 −1.099 −17.858 −6.820 1.00 102.01 C ATOM 4318 C LYS B 334 −1.338 −16.493 −7.466 1.00 111.95 C ATOM 4319 O LYS B 334 −2.040 −16.396 −8.471 1.00 119.51 O ATOM 4320 CB LYS B 334 −2.363 −18.281 −6.066 1.00 112.35 C ATOM 4321 CG LYS B 334 −2.208 −19.496 −5.164 1.00 112.05 C ATOM 4322 CD LYS B 334 −3.257 −19.468 −4.056 1.00 110.60 C ATOM 4323 CE LYS B 334 −3.161 −20.675 −3.138 1.00 101.29 C ATOM 4324 NZ LYS B 334 −4.270 −20.670 −2.140 1.00 97.06 N ATOM 4325 N ALA B 335 −0.771 −15.441 −6.881 1.00 110.97 N ATOM 4326 CA ALA B 335 −0.897 −14.093 −7.439 1.00 111.79 C ATOM 4327 C ALA B 335 0.280 −13.751 −8.361 1.00 121.97 C ATOM 4328 O ALA B 335 0.167 −12.885 −9.234 1.00 109.59 O ATOM 4329 CB ALA B 335 −1.037 −13.052 −6.325 1.00 75.15 C ATOM 4330 N PHE B 336 1.406 −14.436 −8.160 1.00 120.87 N ATOM 4331 CA PHE B 336 2.586 −14.255 −9.006 1.00 119.16 C ATOM 4332 C PHE B 336 2.355 −14.854 −10.398 1.00 118.29 C ATOM 4333 O PHE B 336 2.956 −14.417 −11.380 1.00 102.70 O ATOM 4334 CB PHE B 336 3.835 −14.897 −8.368 1.00 115.86 C ATOM 4335 CG PHE B 336 4.493 −14.055 −7.287 1.00 124.23 C ATOM 4336 CD1 PHE B 336 4.390 −12.667 −7.290 1.00 119.81 C ATOM 4337 CD2 PHE B 336 5.249 −14.660 −6.285 1.00 109.51 C ATOM 4338 CE1 PHE B 336 5.006 −11.900 −6.299 1.00 93.03 C ATOM 4339 CE2 PHE B 336 5.866 −13.901 −5.296 1.00 83.46 C ATOM 4340 CZ PHE B 336 5.744 −12.521 −5.305 1.00 77.61 C ATOM 4341 N LYS B 337 1.480 −15.855 −10.469 1.00 120.39 N ATOM 4342 CA LYS B 337 1.248 −16.599 −11.706 1.00 122.08 C ATOM 4343 C LYS B 337 0.026 −16.108 −12.482 1.00 121.81 C ATOM 4344 O LYS B 337 −0.157 −16.470 −13.643 1.00 125.11 O ATOM 4345 CB LYS B 337 1.121 −18.099 −11.414 1.00 111.45 C ATOM 4346 CG LYS B 337 2.332 −18.691 −10.705 1.00 106.49 C ATOM 4347 CD LYS B 337 1.984 −19.982 −9.981 1.00 113.20 C ATOM 4348 CE LYS B 337 3.102 −20.403 −9.031 1.00 123.56 C ATOM 4349 NZ LYS B 337 2.733 −21.608 −8.224 1.00 100.74 N ATOM 4350 N ARG B 338 −0.807 −15.291 −11.843 1.00 121.29 N ATOM 4351 CA ARG B 338 −1.979 −14.716 −12.508 1.00 121.70 C ATOM 4352 C ARG B 338 −1.600 −13.561 −13.439 1.00 127.12 C ATOM 4353 O ARG B 338 −2.242 −13.341 −14.470 1.00 121.10 O ATOM 4354 CB ARG B 338 −2.998 −14.221 −11.478 1.00 122.50 C ATOM 4355 CG ARG B 338 −3.700 −15.314 −10.700 1.00 130.70 C ATOM 4356 CD ARG B 338 −4.620 −14.713 −9.648 1.00 137.60 C ATOM 4357 NE ARG B 338 −5.348 −15.730 −8.896 1.00 142.59 N ATOM 4358 CZ ARG B 338 −6.368 −15.467 −8.085 1.00 153.95 C ATOM 4359 NH1 ARG B 338 −6.781 −14.216 −7.924 1.00 145.87 N ATOM 4360 NH2 ARG B 338 −6.978 −16.452 −7.437 1.00 162.50 N ATOM 4361 N LEU B 339 −0.560 −12.822 −13.058 1.00 128.05 N ATOM 4362 CA LEU B 339 −0.108 −11.652 −13.811 1.00 120.13 C ATOM 4363 C LEU B 339 0.942 −12.050 −14.854 1.00 121.90 C ATOM 4364 O LEU B 339 1.074 −11.407 −15.899 1.00 105.79 O ATOM 4365 CB LEU B 339 0.453 −10.594 −12.852 1.00 106.20 C ATOM 4366 CG LEU B 339 −0.436 −10.197 −11.663 1.00 96.28 C ATOM 4367 CD1 LEU B 339 0.345 −10.169 −10.352 1.00 79.91 C ATOM 4368 CD2 LEU B 339 −1.130 −8.869 −11.910 1.00 74.91 C ATOM 4369 N LEU B 340 1.687 −13.114 −14.559 1.00 128.17 N ATOM 4370 CA LEU B 340 2.622 −13.703 −15.517 1.00 133.42 C ATOM 4371 C LEU B 340 1.874 −14.658 −16.466 1.00 139.47 C ATOM 4372 O LEU B 340 2.485 −15.321 −17.309 1.00 131.04 O ATOM 4373 CB LEU B 340 3.765 −14.434 −14.787 1.00 127.90 C ATOM 4374 CG LEU B 340 4.846 −13.629 −14.043 1.00 105.66 C ATOM 4375 CD1 LEU B 340 5.413 −14.415 −12.862 1.00 86.15 C ATOM 4376 CD2 LEU B 340 5.970 −13.186 −14.981 1.00 78.32 C ATOM 4377 N ALA B 341 0.550 −14.717 −16.307 1.00 135.84 N ATOM 4378 CA ALA B 341 −0.345 −15.507 −17.165 1.00 126.94 C ATOM 4379 C ALA B 341 0.012 −16.996 −17.297 1.00 143.65 C ATOM 4380 O ALA B 341 0.823 −17.377 −18.145 1.00 137.53 O ATOM 4381 CB ALA B 341 −0.475 −14.859 −18.542 1.00 117.07 C ATOM 4382 N PHE B 342 −0.615 −17.828 −16.464 1.00 148.59 N ATOM 4383 CA PHE B 342 −0.409 −19.279 −16.495 1.00 144.33 C ATOM 4384 C PHE B 342 −1.727 −20.048 −16.445 1.00 130.89 C ATOM 4385 O PHE B 342 −1.807 −21.126 −15.851 1.00 117.74 O ATOM 4386 CB PHE B 342 0.488 −19.730 −15.338 1.00 141.69 C ATOM 4387 CG PHE B 342 1.955 −19.564 −15.606 1.00 137.50 C ATOM 4388 CD1 PHE B 342 2.585 −18.353 −15.364 1.00 143.13 C ATOM 4389 CD2 PHE B 342 2.704 −20.618 −16.098 1.00 143.09 C ATOM 4390 CE1 PHE B 342 3.935 −18.195 −15.611 1.00 137.82 C ATOM 4391 CE2 PHE B 342 4.054 −20.470 −16.346 1.00 152.37 C ATOM 4392 CZ PHE B 342 4.672 −19.254 −16.102 1.00 150.97 C ATOM 4393 C16 PDL B 400 29.184 7.069 4.937 1.00 38.38 C ATOM 4394 N3 PDL B 400 30.198 7.533 5.152 1.00 36.99 N ATOM 4395 N1 PDL B 400 26.640 6.887 5.573 1.00 30.93 N ATOM 4396 C1 PDL B 400 27.850 6.583 4.719 1.00 41.26 C ATOM 4397 C2 PDL B 400 27.442 5.605 3.626 1.00 25.18 C ATOM 4398 C3 PDL B 400 26.003 5.338 3.817 1.00 27.64 C ATOM 4399 C4 PDL B 400 25.030 4.457 3.065 1.00 33.14 C ATOM 4400 C5 PDL B 400 23.560 4.358 3.477 1.00 30.90 C ATOM 4401 C6 PDL B 400 23.064 5.159 4.681 1.00 32.86 C ATOM 4402 C7 PDL B 400 24.036 6.038 5.444 1.00 34.59 C ATOM 4403 C8 PDL B 400 25.503 6.122 5.016 1.00 30.42 C ATOM 4404 O1 PDL B 400 25.519 3.723 1.989 1.00 35.41 O ATOM 4405 C9 PDL B 400 24.720 3.588 0.854 1.00 35.15 C ATOM 4406 C10 PDL B 400 25.620 2.952 −0.198 1.00 27.24 C ATOM 4407 O2 PDL B 400 24.804 2.393 −1.197 1.00 31.27 O ATOM 4408 C11 PDL B 400 26.522 4.071 −0.743 1.00 23.86 C ATOM 4409 N2 PDL B 400 26.911 3.874 −2.133 1.00 36.17 N ATOM 4410 C12 PDL B 400 27.783 4.976 −2.559 1.00 34.60 C ATOM 4411 C13 PDL B 400 28.937 5.154 −1.541 1.00 16.62 C ATOM 4412 C14 PDL B 400 26.994 6.311 −2.646 1.00 28.02 C ATOM 4413 C15 PDL B 400 28.316 4.566 −3.955 1.00 28.75 C ATOM 4414 NA NA B 401 33.452 14.952 −8.392 1.00 48.82 Na

TABLE C CRYST1 55.500 86.800 95.500 67.60 73.30 85.80 P 1 SCALE1 0.018018 −0.001323 −0.005298 0.00000 SCALE2 0.000000 0.011552 −0.004700 0.00000 SCALE3 0.000000 0.000000 0.011803 0.00000 ATOM 4415 N GLN C 31 62.786 46.162 14.725 1.00 73.97 N ATOM 4416 CA GLN C 31 62.534 44.982 13.901 1.00 84.04 C ATOM 4417 C GLN C 31 62.029 45.362 12.511 1.00 79.46 C ATOM 4418 O GLN C 31 60.883 45.781 12.355 1.00 80.45 O ATOM 4419 CB GLN C 31 61.515 44.068 14.578 1.00 65.74 C ATOM 4420 CG GLN C 31 61.854 43.733 16.022 1.00 81.81 C ATOM 4421 CD GLN C 31 60.811 42.840 16.663 1.00 78.61 C ATOM 4422 OE1 GLN C 31 60.080 42.128 15.971 1.00 83.04 O ATOM 4423 NE2 GLN C 31 60.733 42.873 17.989 1.00 53.86 N ATOM 4424 N TRP C 32 62.876 45.202 11.499 1.00 80.99 N ATOM 4425 CA TRP C 32 62.469 45.527 10.143 1.00 66.35 C ATOM 4426 C TRP C 32 61.316 44.607 9.725 1.00 71.15 C ATOM 4427 O TRP C 32 60.527 44.950 8.848 1.00 76.04 O ATOM 4428 CB TRP C 32 63.668 45.409 9.205 1.00 60.12 C ATOM 4429 CG TRP C 32 63.348 45.401 7.752 1.00 81.94 C ATOM 4430 CD1 TRP C 32 63.301 46.481 6.915 1.00 88.94 C ATOM 4431 CD2 TRP C 32 63.067 44.249 6.941 1.00 84.57 C ATOM 4432 NE1 TRP C 32 62.993 46.073 5.637 1.00 99.22 N ATOM 4433 CE2 TRP C 32 62.843 44.709 5.625 1.00 96.78 C ATOM 4434 CE3 TRP C 32 62.970 42.877 7.205 1.00 65.06 C ATOM 4435 CZ2 TRP C 32 62.526 43.840 4.568 1.00 78.58 C ATOM 4436 CZ3 TRP C 32 62.657 42.017 6.158 1.00 66.47 C ATOM 4437 CH2 TRP C 32 62.438 42.504 4.855 1.00 66.98 C ATOM 4438 N GLU C 33 61.215 43.450 10.377 1.00 68.90 N ATOM 4439 CA GLU C 33 60.117 42.510 10.151 1.00 59.18 C ATOM 4440 C GLU C 33 58.768 43.096 10.535 1.00 58.54 C ATOM 4441 O GLU C 33 57.749 42.745 9.954 1.00 60.57 O ATOM 4442 CB GLU C 33 60.324 41.214 10.949 1.00 59.21 C ATOM 4443 CG GLU C 33 59.060 40.340 11.045 1.00 62.28 C ATOM 4444 CD GLU C 33 59.191 39.145 11.997 1.00 78.60 C ATOM 4445 OE1 GLU C 33 60.246 39.002 12.653 1.00 81.38 O ATOM 4446 OE2 GLU C 33 58.229 38.342 12.090 1.00 63.82 O ATOM 4447 N ALA C 34 58.759 43.979 11.526 1.00 71.57 N ATOM 4448 CA ALA C 34 57.508 44.516 12.063 1.00 65.77 C ATOM 4449 C ALA C 34 56.901 45.614 11.187 1.00 70.86 C ATOM 4450 O ALA C 34 55.682 45.663 11.004 1.00 68.62 O ATOM 4451 CB ALA C 34 57.712 45.019 13.478 1.00 63.35 C ATOM 4452 N GLY C 35 57.745 46.494 10.651 1.00 66.41 N ATOM 4453 CA GLY C 35 57.276 47.540 9.759 1.00 52.59 C ATOM 4454 C GLY C 35 56.802 46.950 8.446 1.00 59.86 C ATOM 4455 O GLY C 35 55.877 47.456 7.813 1.00 60.33 O ATOM 4456 N MET C 36 57.449 45.865 8.040 1.00 60.06 N ATOM 4457 CA MET C 36 57.107 45.173 6.808 1.00 56.81 C ATOM 4458 C MET C 36 55.742 44.484 6.947 1.00 62.32 C ATOM 4459 O MET C 36 54.906 44.555 6.048 1.00 66.44 O ATOM 4460 CB MET C 36 58.213 44.174 6.449 1.00 54.32 C ATOM 4461 CG MET C 36 58.453 43.990 4.949 1.00 83.69 C ATOM 4462 SD MET C 36 58.945 45.492 4.053 1.00 79.58 S ATOM 4463 CE MET C 36 59.989 46.285 5.275 1.00 78.14 C ATOM 4464 N SER C 37 55.510 43.842 8.088 1.00 62.46 N ATOM 4465 CA SER C 37 54.224 43.208 8.372 1.00 50.69 C ATOM 4466 C SER C 37 53.137 44.256 8.544 1.00 55.16 C ATOM 4467 O SER C 37 51.961 43.929 8.705 1.00 51.21 O ATOM 4468 CB SER C 37 54.304 42.361 9.646 1.00 50.62 C ATOM 4469 OG SER C 37 55.345 41.402 9.581 1.00 58.02 O ATOM 4470 N LEU C 38 53.532 45.521 8.532 1.00 66.77 N ATOM 4471 CA LEU C 38 52.566 46.599 8.665 1.00 62.24 C ATOM 4472 C LEU C 38 52.107 47.083 7.290 1.00 60.02 C ATOM 4473 O LEU C 38 50.908 47.096 7.011 1.00 57.78 O ATOM 4474 CB LEU C 38 53.140 47.752 9.480 1.00 64.47 C ATOM 4475 CG LEU C 38 52.074 48.539 10.239 1.00 74.81 C ATOM 4476 CD1 LEU C 38 51.615 47.749 11.450 1.00 59.27 C ATOM 4477 CD2 LEU C 38 52.612 49.888 10.653 1.00 75.98 C ATOM 4478 N LEU C 39 53.049 47.470 6.431 1.00 54.36 N ATOM 4479 CA LEU C 39 52.690 47.874 5.071 1.00 72.39 C ATOM 4480 C LEU C 39 52.065 46.714 4.309 1.00 62.03 C ATOM 4481 O LEU C 39 51.230 46.909 3.426 1.00 62.94 O ATOM 4482 CB LEU C 39 53.887 48.439 4.286 1.00 78.71 C ATOM 4483 CG LEU C 39 54.230 49.934 4.429 1.00 96.84 C ATOM 4484 CD1 LEU C 39 54.644 50.534 3.079 1.00 76.04 C ATOM 4485 CD2 LEU C 39 53.074 50.742 5.028 1.00 76.37 C ATOM 4486 N MET C 40 52.470 45.501 4.654 1.00 61.96 N ATOM 4487 CA MET C 40 51.911 44.332 4.003 1.00 56.57 C ATOM 4488 C MET C 40 50.470 44.158 4.473 1.00 47.73 C ATOM 4489 O MET C 40 49.551 44.058 3.664 1.00 47.30 O ATOM 4490 CB MET C 40 52.758 43.093 4.299 1.00 45.62 C ATOM 4491 CG MET C 40 53.064 42.248 3.063 1.00 52.12 C ATOM 4492 SD MET C 40 54.007 43.090 1.764 1.00 77.40 S ATOM 4493 CE MET C 40 55.643 43.128 2.494 1.00 75.54 C ATOM 4494 N ALA C 41 50.275 44.153 5.785 1.00 41.08 N ATOM 4495 CA ALA C 41 48.939 44.066 6.345 1.00 41.50 C ATOM 4496 C ALA C 41 48.034 45.152 5.756 1.00 46.54 C ATOM 4497 O ALA C 41 46.817 44.976 5.657 1.00 36.41 O ATOM 4498 CB ALA C 41 49.004 44.180 7.846 1.00 34.26 C ATOM 4499 N LEU C 42 48.641 46.265 5.358 1.00 48.53 N ATOM 4500 CA LEU C 42 47.901 47.400 4.818 1.00 51.39 C ATOM 4501 C LEU C 42 47.378 47.125 3.413 1.00 52.74 C ATOM 4502 O LEU C 42 46.209 47.380 3.121 1.00 52.16 O ATOM 4503 CB LEU C 42 48.782 48.647 4.781 1.00 63.53 C ATOM 4504 CG LEU C 42 48.034 49.975 4.871 1.00 68.94 C ATOM 4505 CD1 LEU C 42 47.935 50.383 6.336 1.00 50.82 C ATOM 4506 CD2 LEU C 42 48.727 51.051 4.049 1.00 59.08 C ATOM 4507 N VAL C 43 48.248 46.618 2.542 1.00 47.79 N ATOM 4508 CA VAL C 43 47.838 46.288 1.181 1.00 43.61 C ATOM 4509 C VAL C 43 46.746 45.229 1.195 1.00 41.83 C ATOM 4510 O VAL C 43 45.739 45.369 0.506 1.00 48.48 O ATOM 4511 CB VAL C 43 49.019 45.830 0.286 1.00 41.39 C ATOM 4512 CG1 VAL C 43 50.086 46.897 0.232 1.00 44.46 C ATOM 4513 CG2 VAL C 43 49.606 44.536 0.789 1.00 47.99 C ATOM 4514 N VAL C 44 46.932 44.179 1.988 1.00 33.84 N ATOM 4515 CA VAL C 44 45.909 43.149 2.104 1.00 34.68 C ATOM 4516 C VAL C 44 44.562 43.792 2.440 1.00 43.41 C ATOM 4517 O VAL C 44 43.510 43.337 1.991 1.00 38.69 O ATOM 4518 CB VAL C 44 46.277 42.111 3.170 1.00 27.15 C ATOM 4519 CG1 VAL C 44 45.091 41.206 3.467 1.00 21.09 C ATOM 4520 CG2 VAL C 44 47.479 41.304 2.732 1.00 31.64 C ATOM 4521 N LEU C 45 44.614 44.871 3.217 1.00 48.46 N ATOM 4522 CA LEU C 45 43.413 45.596 3.621 1.00 52.10 C ATOM 4523 C LEU C 45 42.768 46.351 2.460 1.00 44.83 C ATOM 4524 O LEU C 45 41.555 46.287 2.267 1.00 40.42 O ATOM 4525 CB LEU C 45 43.739 46.579 4.745 1.00 57.12 C ATOM 4526 CG LEU C 45 42.544 47.444 5.140 1.00 56.39 C ATOM 4527 CD1 LEU C 45 41.495 46.578 5.810 1.00 48.18 C ATOM 4528 CD2 LEU C 45 42.972 48.591 6.037 1.00 44.29 C ATOM 4529 N LEU C 46 43.585 47.093 1.716 1.00 41.67 N ATOM 4530 CA LEU C 46 43.137 47.744 0.493 1.00 42.00 C ATOM 4531 C LEU C 46 42.459 46.739 −0.430 1.00 49.10 C ATOM 4532 O LEU C 46 41.241 46.775 −0.609 1.00 50.26 O ATOM 4533 CB LEU C 46 44.323 48.369 −0.233 1.00 45.05 C ATOM 4534 CG LEU C 46 44.596 49.837 0.060 1.00 48.17 C ATOM 4535 CD1 LEU C 46 45.698 50.364 −0.852 1.00 44.38 C ATOM 4536 CD2 LEU C 46 43.314 50.621 −0.140 1.00 55.66 C ATOM 4537 N ILE C 47 43.262 45.843 −1.005 1.00 43.20 N ATOM 4538 CA ILE C 47 42.770 44.787 −1.884 1.00 48.27 C ATOM 4539 C ILE C 47 41.515 44.100 −1.356 1.00 40.95 C ATOM 4540 O ILE C 47 40.548 43.928 −2.090 1.00 44.08 O ATOM 4541 CB ILE C 47 43.835 43.693 −2.128 1.00 48.44 C ATOM 4542 CG1 ILE C 47 45.103 44.298 −2.727 1.00 41.36 C ATOM 4543 CG2 ILE C 47 43.285 42.594 −3.038 1.00 34.31 C ATOM 4544 CD1 ILE C 47 46.295 43.371 −2.650 1.00 37.34 C ATOM 4545 N VAL C 48 41.523 43.687 −0.097 1.00 32.06 N ATOM 4546 CA VAL C 48 40.371 42.950 0.398 1.00 38.94 C ATOM 4547 C VAL C 48 39.137 43.828 0.573 1.00 46.74 C ATOM 4548 O VAL C 48 38.031 43.430 0.201 1.00 52.34 O ATOM 4549 CB VAL C 48 40.645 42.183 1.695 1.00 34.72 C ATOM 4550 CG1 VAL C 48 39.333 41.632 2.235 1.00 31.10 C ATOM 4551 CG2 VAL C 48 41.630 41.046 1.442 1.00 31.62 C ATOM 4552 N ALA C 49 39.317 45.022 1.127 1.00 48.15 N ATOM 4553 CA ALA C 49 38.181 45.913 1.353 1.00 49.66 C ATOM 4554 C ALA C 49 37.560 46.410 0.039 1.00 50.65 C ATOM 4555 O ALA C 49 36.343 46.339 −0.162 1.00 42.51 O ATOM 4556 CB ALA C 49 38.585 47.082 2.232 1.00 32.74 C ATOM 4557 N GLY C 50 38.402 46.910 −0.855 1.00 44.28 N ATOM 4558 CA GLY C 50 37.925 47.496 −2.092 1.00 50.62 C ATOM 4559 C GLY C 50 37.223 46.512 −3.005 1.00 49.92 C ATOM 4560 O GLY C 50 36.278 46.863 −3.709 1.00 54.95 O ATOM 4561 N ASN C 51 37.687 45.272 −3.006 1.00 45.78 N ATOM 4562 CA ASN C 51 37.132 44.283 −3.908 1.00 42.07 C ATOM 4563 C ASN C 51 35.901 43.627 −3.330 1.00 45.47 C ATOM 4564 O ASN C 51 35.089 43.076 −4.063 1.00 54.88 O ATOM 4565 CB ASN C 51 38.178 43.235 −4.265 1.00 44.54 C ATOM 4566 CG ASN C 51 39.097 43.696 −5.368 1.00 50.86 C ATOM 4567 OD1 ASN C 51 38.698 43.755 −6.533 1.00 48.17 O ATOM 4568 ND2 ASN C 51 40.340 44.033 −5.011 1.00 47.17 N ATOM 4569 N VAL C 52 35.768 43.677 −2.012 1.00 39.71 N ATOM 4570 CA VAL C 52 34.572 43.164 −1.372 1.00 45.09 C ATOM 4571 C VAL C 52 33.490 44.220 −1.533 1.00 46.91 C ATOM 4572 O VAL C 52 32.300 43.912 −1.609 1.00 42.98 O ATOM 4573 CB VAL C 52 34.829 42.824 0.117 1.00 41.79 C ATOM 4574 CG1 VAL C 52 33.526 42.705 0.889 1.00 21.89 C ATOM 4575 CG2 VAL C 52 35.624 41.538 0.231 1.00 37.43 C ATOM 4576 N LEU C 53 33.937 45.470 −1.611 1.00 50.38 N ATOM 4577 CA LEU C 53 33.069 46.623 −1.821 1.00 51.68 C ATOM 4578 C LEU C 53 32.412 46.549 −3.192 1.00 53.17 C ATOM 4579 O LEU C 53 31.200 46.699 −3.324 1.00 53.58 O ATOM 4580 CB LEU C 53 33.899 47.901 −1.728 1.00 59.29 C ATOM 4581 CG LEU C 53 33.299 49.057 −0.935 1.00 69.13 C ATOM 4582 CD1 LEU C 53 32.797 48.562 0.414 1.00 52.50 C ATOM 4583 CD2 LEU C 53 34.342 50.143 −0.754 1.00 78.61 C ATOM 4584 N VAL C 54 33.233 46.319 −4.210 1.00 54.77 N ATOM 4585 CA VAL C 54 32.756 46.140 −5.571 1.00 48.50 C ATOM 4586 C VAL C 54 31.727 45.015 −5.661 1.00 50.61 C ATOM 4587 O VAL C 54 30.598 45.234 −6.084 1.00 52.82 O ATOM 4588 CB VAL C 54 33.920 45.844 −6.522 1.00 45.32 C ATOM 4589 CG1 VAL C 54 33.403 45.432 −7.895 1.00 50.00 C ATOM 4590 CG2 VAL C 54 34.835 47.055 −6.621 1.00 45.78 C ATOM 4591 N ILE C 55 32.119 43.814 −5.255 1.00 47.56 N ATOM 4592 CA ILE C 55 31.236 42.657 −5.337 1.00 49.13 C ATOM 4593 C ILE C 55 29.918 42.898 −4.618 1.00 54.45 C ATOM 4594 O ILE C 55 28.860 42.471 −5.082 1.00 65.43 O ATOM 4595 CB ILE C 55 31.889 41.392 −4.760 1.00 48.28 C ATOM 4596 CG1 ILE C 55 33.024 40.910 −5.671 1.00 44.06 C ATOM 4597 CG2 ILE C 55 30.854 40.299 −4.584 1.00 36.19 C ATOM 4598 CD1 ILE C 55 34.054 40.027 −4.964 1.00 37.14 C ATOM 4599 N ALA C 56 29.973 43.587 −3.487 1.00 54.42 N ATOM 4600 CA ALA C 56 28.755 43.862 −2.727 1.00 54.56 C ATOM 4601 C ALA C 56 27.909 44.959 −3.369 1.00 56.07 C ATOM 4602 O ALA C 56 26.687 44.858 −3.409 1.00 58.96 O ATOM 4603 CB ALA C 56 29.090 44.216 −1.300 1.00 40.87 C ATOM 4604 N ALA C 57 28.561 46.002 −3.876 1.00 54.31 N ATOM 4605 CA ALA C 57 27.854 47.107 −4.522 1.00 60.09 C ATOM 4606 C ALA C 57 27.045 46.625 −5.721 1.00 72.86 C ATOM 4607 O ALA C 57 25.888 47.008 −5.898 1.00 77.43 O ATOM 4608 CB ALA C 57 28.832 48.188 −4.950 1.00 57.46 C ATOM 4609 N ILE C 58 27.668 45.790 −6.546 1.00 72.60 N ATOM 4610 CA ILE C 58 27.006 45.216 −7.707 1.00 68.68 C ATOM 4611 C ILE C 58 25.900 44.279 −7.243 1.00 65.99 C ATOM 4612 O ILE C 58 24.821 44.236 −7.827 1.00 77.27 O ATOM 4613 CB ILE C 58 28.012 44.478 −8.617 1.00 54.52 C ATOM 4614 CG1 ILE C 58 28.961 45.483 −9.260 1.00 46.71 C ATOM 4615 CG2 ILE C 58 27.298 43.684 −9.700 1.00 47.13 C ATOM 4616 CD1 ILE C 58 30.109 44.845 −10.001 1.00 54.09 C ATOM 4617 N GLY C 59 26.169 43.545 −6.172 1.00 64.64 N ATOM 4618 CA GLY C 59 25.177 42.655 −5.599 1.00 82.78 C ATOM 4619 C GLY C 59 23.985 43.392 −5.011 1.00 90.05 C ATOM 4620 O GLY C 59 22.879 42.851 −4.951 1.00 83.53 O ATOM 4621 N SER C 60 24.211 44.630 −4.577 1.00 91.68 N ATOM 4622 CA SER C 60 23.163 45.430 −3.945 1.00 94.42 C ATOM 4623 C SER C 60 22.216 46.046 −4.970 1.00 88.91 C ATOM 4624 O SER C 60 21.043 45.683 −5.033 1.00 109.21 O ATOM 4625 CB SER C 60 23.770 46.522 −3.057 1.00 74.97 C ATOM 4626 OG SER C 60 24.478 45.949 −1.971 1.00 72.49 O ATOM 4627 N THR C 61 22.727 46.975 −5.768 1.00 82.88 N ATOM 4628 CA THR C 61 21.926 47.618 −6.804 1.00 99.39 C ATOM 4629 C THR C 61 21.803 46.724 −8.036 1.00 109.99 C ATOM 4630 O THR C 61 22.806 46.204 −8.531 1.00 109.28 O ATOM 4631 CB THR C 61 22.562 48.949 −7.250 1.00 107.69 C ATOM 4632 OG1 THR C 61 23.376 49.477 −6.193 1.00 104.62 O ATOM 4633 CG2 THR C 61 21.486 49.963 −7.638 1.00 103.40 C ATOM 4634 N GLN C 62 20.582 46.543 −8.534 1.00 106.69 N ATOM 4635 CA GLN C 62 20.394 45.846 −9.804 1.00 111.46 C ATOM 4636 C GLN C 62 20.655 46.838 −10.924 1.00 106.79 C ATOM 4637 O GLN C 62 20.941 46.455 −12.062 1.00 93.82 O ATOM 4638 CB GLN C 62 18.979 45.301 −9.933 1.00 117.58 C ATOM 4639 CG GLN C 62 18.398 44.766 −8.651 1.00 121.59 C ATOM 4640 CD GLN C 62 16.909 45.011 −8.577 1.00 102.55 C ATOM 4641 OE1 GLN C 62 16.301 45.472 −9.545 1.00 85.70 O ATOM 4642 NE2 GLN C 62 16.312 44.714 −7.426 1.00 96.22 N ATOM 4643 N ARG C 63 20.533 48.120 −10.593 1.00 100.21 N ATOM 4644 CA ARG C 63 20.925 49.179 −11.505 1.00 97.55 C ATOM 4645 C ARG C 63 22.375 48.945 −11.924 1.00 105.03 C ATOM 4646 O ARG C 63 22.715 49.008 −13.111 1.00 90.47 O ATOM 4647 CB ARG C 63 20.788 50.540 −10.830 1.00 85.16 C ATOM 4648 CG ARG C 63 21.132 51.692 −11.741 1.00 106.18 C ATOM 4649 CD ARG C 63 21.392 52.963 −10.969 1.00 113.67 C ATOM 4650 NE ARG C 63 21.821 54.036 −11.861 1.00 132.81 N ATOM 4651 CZ ARG C 63 22.111 55.269 −11.462 1.00 144.18 C ATOM 4652 NH1 ARG C 63 22.020 55.593 −10.180 1.00 147.80 N ATOM 4653 NH2 ARG C 63 22.493 56.181 −12.348 1.00 139.74 N ATOM 4654 N LEU C 64 23.223 48.668 −10.936 1.00 103.38 N ATOM 4655 CA LEU C 64 24.613 48.303 −11.188 1.00 95.78 C ATOM 4656 C LEU C 64 24.749 46.897 −11.793 1.00 90.56 C ATOM 4657 O LEU C 64 25.809 46.533 −12.295 1.00 77.59 O ATOM 4658 CB LEU C 64 25.441 48.406 −9.901 1.00 90.67 C ATOM 4659 CG LEU C 64 26.122 49.737 −9.569 1.00 91.86 C ATOM 4660 CD1 LEU C 64 26.961 49.613 −8.298 1.00 83.68 C ATOM 4661 CD2 LEU C 64 26.987 50.201 −10.730 1.00 70.29 C ATOM 4662 N GLN C 65 23.685 46.101 −11.743 1.00 87.87 N ATOM 4663 CA GLN C 65 23.736 44.775 −12.354 1.00 83.74 C ATOM 4664 C GLN C 65 23.481 44.803 −13.859 1.00 89.14 C ATOM 4665 O GLN C 65 22.353 44.633 −14.324 1.00 86.62 O ATOM 4666 CB GLN C 65 22.797 43.791 −11.659 1.00 94.05 C ATOM 4667 CG GLN C 65 23.522 42.784 −10.786 1.00 86.15 C ATOM 4668 CD GLN C 65 22.573 41.876 −10.033 1.00 100.19 C ATOM 4669 OE1 GLN C 65 21.368 42.135 −9.960 1.00 110.17 O ATOM 4670 NE2 GLN C 65 23.113 40.804 −9.464 1.00 84.23 N ATOM 4671 N THR C 66 24.553 45.041 −14.604 1.00 75.73 N ATOM 4672 CA THR C 66 24.552 44.922 −16.045 1.00 46.63 C ATOM 4673 C THR C 66 25.315 43.647 −16.346 1.00 54.00 C ATOM 4674 O THR C 66 25.679 42.918 −15.427 1.00 65.51 O ATOM 4675 CB THR C 66 25.311 46.084 −16.680 1.00 56.30 C ATOM 4676 OG1 THR C 66 26.700 45.968 −16.350 1.00 55.23 O ATOM 4677 CG2 THR C 66 24.789 47.410 −16.161 1.00 48.65 C ATOM 4678 N LEU C 67 25.562 43.370 −17.624 1.00 55.05 N ATOM 4679 CA LEU C 67 26.374 42.217 −18.001 1.00 45.27 C ATOM 4680 C LEU C 67 27.832 42.534 −17.754 1.00 52.34 C ATOM 4681 O LEU C 67 28.567 41.729 −17.179 1.00 52.53 O ATOM 4682 CB LEU C 67 26.198 41.883 −19.478 1.00 55.93 C ATOM 4683 CG LEU C 67 25.033 40.995 −19.888 1.00 48.38 C ATOM 4684 CD1 LEU C 67 25.273 40.502 −21.304 1.00 58.75 C ATOM 4685 CD2 LEU C 67 24.899 39.833 −18.917 1.00 43.87 C ATOM 4686 N THR C 68 28.239 43.715 −18.212 1.00 46.53 N ATOM 4687 CA THR C 68 29.600 44.200 −18.038 1.00 41.22 C ATOM 4688 C THR C 68 30.063 44.013 −16.603 1.00 45.68 C ATOM 4689 O THR C 68 31.199 43.601 −16.355 1.00 49.05 O ATOM 4690 CB THR C 68 29.713 45.696 −18.395 1.00 51.69 C ATOM 4691 OG1 THR C 68 29.587 45.867 −19.813 1.00 55.23 O ATOM 4692 CG2 THR C 68 31.058 46.266 −17.929 1.00 44.27 C ATOM 4693 N ASN C 69 29.172 44.312 −15.661 1.00 41.66 N ATOM 4694 CA ASN C 69 29.505 44.249 −14.250 1.00 41.97 C ATOM 4695 C ASN C 69 29.567 42.828 −13.724 1.00 40.00 C ATOM 4696 O ASN C 69 30.156 42.568 −12.673 1.00 39.29 O ATOM 4697 CB ASN C 69 28.532 45.097 −13.435 1.00 55.42 C ATOM 4698 CG ASN C 69 28.748 46.575 −13.650 1.00 48.66 C ATOM 4699 OD1 ASN C 69 29.749 46.982 −14.231 1.00 51.76 O ATOM 4700 ND2 ASN C 69 27.811 47.385 −13.192 1.00 60.90 N ATOM 4701 N LEU C 70 28.961 41.909 −14.464 1.00 37.66 N ATOM 4702 CA LEU C 70 29.108 40.490 −14.174 1.00 43.55 C ATOM 4703 C LEU C 70 30.544 40.038 −14.405 1.00 40.21 C ATOM 4704 O LEU C 70 31.101 39.291 −13.598 1.00 28.53 O ATOM 4705 CB LEU C 70 28.149 39.669 −15.029 1.00 51.13 C ATOM 4706 CG LEU C 70 26.717 39.715 −14.510 1.00 47.35 C ATOM 4707 CD1 LEU C 70 25.864 38.659 −15.206 1.00 44.90 C ATOM 4708 CD2 LEU C 70 26.736 39.511 −12.996 1.00 32.10 C ATOM 4709 N PHE C 71 31.136 40.504 −15.506 1.00 38.89 N ATOM 4710 CA PHE C 71 32.535 40.214 −15.804 1.00 41.67 C ATOM 4711 C PHE C 71 33.476 40.943 −14.853 1.00 36.73 C ATOM 4712 O PHE C 71 34.544 40.433 −14.515 1.00 33.70 O ATOM 4713 CB PHE C 71 32.866 40.527 −17.264 1.00 41.41 C ATOM 4714 CG PHE C 71 32.045 39.738 −18.241 1.00 39.93 C ATOM 4715 CD1 PHE C 71 31.839 38.382 −18.046 1.00 38.30 C ATOM 4716 CD2 PHE C 71 31.476 40.350 −19.352 1.00 43.04 C ATOM 4717 CE1 PHE C 71 31.069 37.646 −18.929 1.00 44.22 C ATOM 4718 CE2 PHE C 71 30.708 39.627 −20.240 1.00 36.61 C ATOM 4719 CZ PHE C 71 30.502 38.268 −20.028 1.00 41.31 C ATOM 4720 N ILE C 72 33.058 42.128 −14.415 1.00 40.69 N ATOM 4721 CA ILE C 72 33.784 42.904 −13.411 1.00 39.23 C ATOM 4722 C ILE C 72 33.826 42.188 −12.062 1.00 33.50 C ATOM 4723 O ILE C 72 34.815 42.259 −11.335 1.00 33.81 O ATOM 4724 CB ILE C 72 33.136 44.278 −13.217 1.00 39.52 C ATOM 4725 CG1 ILE C 72 33.377 45.151 −14.446 1.00 40.15 C ATOM 4726 CG2 ILE C 72 33.673 44.955 −11.980 1.00 38.97 C ATOM 4727 CD1 ILE C 72 34.695 45.813 −14.452 1.00 39.12 C ATOM 4728 N THR C 73 32.745 41.503 −11.723 1.00 34.11 N ATOM 4729 CA THR C 73 32.714 40.734 −10.489 1.00 34.76 C ATOM 4730 C THR C 73 33.728 39.607 −10.567 1.00 36.07 C ATOM 4731 O THR C 73 34.427 39.313 −9.594 1.00 30.89 O ATOM 4732 CB THR C 73 31.317 40.134 −10.225 1.00 41.43 C ATOM 4733 OG1 THR C 73 30.368 41.189 −10.007 1.00 38.58 O ATOM 4734 CG2 THR C 73 31.356 39.233 −9.004 1.00 36.46 C ATOM 4735 N SER C 74 33.794 38.976 −11.737 1.00 37.38 N ATOM 4736 CA SER C 74 34.726 37.882 −11.972 1.00 36.06 C ATOM 4737 C SER C 74 36.137 38.385 −11.714 1.00 34.33 C ATOM 4738 O SER C 74 36.956 37.718 −11.076 1.00 30.56 O ATOM 4739 CB SER C 74 34.588 37.377 −13.406 1.00 31.77 C ATOM 4740 OG SER C 74 35.537 36.363 −13.675 1.00 42.61 O ATOM 4741 N LEU C 75 36.394 39.585 −12.213 1.00 32.95 N ATOM 4742 CA LEU C 75 37.642 40.284 −11.988 1.00 29.89 C ATOM 4743 C LEU C 75 37.867 40.526 −10.493 1.00 36.80 C ATOM 4744 O LEU C 75 38.954 40.263 −9.975 1.00 40.37 O ATOM 4745 CB LEU C 75 37.606 41.610 −12.734 1.00 36.02 C ATOM 4746 CG LEU C 75 38.870 42.037 −13.460 1.00 34.26 C ATOM 4747 CD1 LEU C 75 39.428 40.859 −14.215 1.00 38.09 C ATOM 4748 CD2 LEU C 75 38.535 43.187 −14.396 1.00 34.71 C ATOM 4749 N ALA C 76 36.837 41.019 −9.802 1.00 32.29 N ATOM 4750 CA ALA C 76 36.919 41.263 −8.362 1.00 33.46 C ATOM 4751 C ALA C 76 37.298 40.005 −7.573 1.00 36.45 C ATOM 4752 O ALA C 76 38.142 40.054 −6.683 1.00 39.30 O ATOM 4753 CB ALA C 76 35.617 41.838 −7.843 1.00 32.92 C ATOM 4754 N CYS C 77 36.665 38.883 −7.896 1.00 37.86 N ATOM 4755 CA CYS C 77 36.959 37.624 −7.219 1.00 28.59 C ATOM 4756 C CYS C 77 38.407 37.185 −7.410 1.00 27.56 C ATOM 4757 O CYS C 77 39.012 36.641 −6.500 1.00 26.38 O ATOM 4758 CB CYS C 77 36.020 36.519 −7.695 1.00 22.07 C ATOM 4759 SG CYS C 77 34.333 36.688 −7.110 1.00 54.98 S ATOM 4760 N ALA C 78 38.971 37.408 −8.590 1.00 27.61 N ATOM 4761 CA ALA C 78 40.354 37.019 −8.799 1.00 30.16 C ATOM 4762 C ALA C 78 41.286 37.923 −8.002 1.00 34.87 C ATOM 4763 O ALA C 78 42.349 37.493 −7.573 1.00 42.66 O ATOM 4764 CB ALA C 78 40.720 37.017 −10.273 1.00 25.50 C ATOM 4765 N ASP C 79 40.891 39.173 −7.790 1.00 33.82 N ATOM 4766 CA ASP C 79 41.682 40.063 −6.945 1.00 31.82 C ATOM 4767 C ASP C 79 41.534 39.691 −5.459 1.00 38.56 C ATOM 4768 O ASP C 79 42.473 39.863 −4.666 1.00 36.01 O ATOM 4769 CB ASP C 79 41.314 41.523 −7.205 1.00 31.96 C ATOM 4770 CG ASP C 79 41.646 41.967 −8.631 1.00 56.44 C ATOM 4771 OD1 ASP C 79 42.701 41.539 −9.161 1.00 50.52 O ATOM 4772 OD2 ASP C 79 40.856 42.749 −9.221 1.00 60.23 O ATOM 4773 N LEU C 80 40.367 39.156 −5.097 1.00 24.84 N ATOM 4774 CA LEU C 80 40.112 38.714 −3.736 1.00 29.68 C ATOM 4775 C LEU C 80 40.980 37.517 −3.342 1.00 36.33 C ATOM 4776 O LEU C 80 41.661 37.542 −2.317 1.00 39.93 O ATOM 4777 CB LEU C 80 38.636 38.373 −3.554 1.00 42.03 C ATOM 4778 CG LEU C 80 38.074 38.665 −2.163 1.00 41.32 C ATOM 4779 CD1 LEU C 80 38.262 40.137 −1.806 1.00 37.47 C ATOM 4780 CD2 LEU C 80 36.612 38.276 −2.110 1.00 31.16 C ATOM 4781 N VAL C 81 40.950 36.464 −4.148 1.00 37.74 N ATOM 4782 CA VAL C 81 41.862 35.345 −3.946 1.00 40.81 C ATOM 4783 C VAL C 81 43.286 35.851 −3.674 1.00 32.99 C ATOM 4784 O VAL C 81 43.947 35.371 −2.763 1.00 30.15 O ATOM 4785 CB VAL C 81 41.851 34.363 −5.157 1.00 43.77 C ATOM 4786 CG1 VAL C 81 42.794 33.194 −4.913 1.00 30.80 C ATOM 4787 CG2 VAL C 81 40.434 33.851 −5.425 1.00 31.09 C ATOM 4788 N VAL C 82 43.749 36.825 −4.455 1.00 29.08 N ATOM 4789 CA VAL C 82 45.098 37.374 −4.275 1.00 37.68 C ATOM 4790 C VAL C 82 45.284 38.080 −2.926 1.00 38.64 C ATOM 4791 O VAL C 82 46.281 37.869 −2.236 1.00 33.33 O ATOM 4792 CB VAL C 82 45.488 38.350 −5.418 1.00 33.44 C ATOM 4793 CG1 VAL C 82 46.799 39.073 −5.091 1.00 28.86 C ATOM 4794 CG2 VAL C 82 45.603 37.605 −6.729 1.00 28.54 C ATOM 4795 N GLY C 83 44.327 38.925 −2.562 1.00 34.47 N ATOM 4796 CA GLY C 83 44.392 39.619 −1.292 1.00 41.60 C ATOM 4797 C GLY C 83 44.293 38.679 −0.102 1.00 33.76 C ATOM 4798 O GLY C 83 44.853 38.944 0.956 1.00 26.96 O ATOM 4799 N LEU C 84 43.570 37.580 −0.284 1.00 34.34 N ATOM 4800 CA LEU C 84 43.339 36.609 0.781 1.00 33.08 C ATOM 4801 C LEU C 84 44.379 35.484 0.831 1.00 36.04 C ATOM 4802 O LEU C 84 44.785 35.071 1.911 1.00 36.95 O ATOM 4803 CB LEU C 84 41.945 35.992 0.645 1.00 35.32 C ATOM 4804 CG LEU C 84 40.724 36.847 0.960 1.00 33.50 C ATOM 4805 CD1 LEU C 84 39.481 35.978 0.889 1.00 23.24 C ATOM 4806 CD2 LEU C 84 40.860 37.499 2.333 1.00 31.04 C ATOM 4807 N LEU C 85 44.800 34.975 −0.326 1.00 34.06 N ATOM 4808 CA LEU C 85 45.745 33.856 −0.352 1.00 29.53 C ATOM 4809 C LEU C 85 47.128 34.196 −0.907 1.00 31.87 C ATOM 4810 O LEU C 85 48.138 33.958 −0.249 1.00 38.80 O ATOM 4811 CB LEU C 85 45.149 32.660 −1.088 1.00 30.03 C ATOM 4812 CG LEU C 85 43.919 32.116 −0.369 1.00 33.08 C ATOM 4813 CD1 LEU C 85 43.355 30.878 −1.025 1.00 32.71 C ATOM 4814 CD2 LEU C 85 44.284 31.819 1.060 1.00 39.71 C ATOM 4815 N VAL C 86 47.183 34.757 −2.105 1.00 30.65 N ATOM 4816 CA VAL C 86 48.470 34.985 −2.748 1.00 32.54 C ATOM 4817 C VAL C 86 49.394 35.916 −1.953 1.00 30.57 C ATOM 4818 O VAL C 86 50.487 35.506 −1.579 1.00 28.13 O ATOM 4819 CB VAL C 86 48.311 35.474 −4.192 1.00 25.61 C ATOM 4820 CG1 VAL C 86 49.668 35.506 −4.881 1.00 28.73 C ATOM 4821 CG2 VAL C 86 47.351 34.573 −4.925 1.00 21.50 C ATOM 4822 N VAL C 87 48.952 37.146 −1.678 1.00 35.92 N ATOM 4823 CA VAL C 87 49.810 38.143 −1.019 1.00 32.25 C ATOM 4824 C VAL C 87 50.179 37.778 0.419 1.00 37.01 C ATOM 4825 O VAL C 87 51.334 37.930 0.811 1.00 41.30 O ATOM 4826 CB VAL C 87 49.211 39.570 −1.054 1.00 34.14 C ATOM 4827 CG1 VAL C 87 49.817 40.429 0.059 1.00 27.39 C ATOM 4828 CG2 VAL C 87 49.425 40.211 −2.422 1.00 28.56 C ATOM 4829 N PRO C 88 49.201 37.313 1.216 1.00 34.86 N ATOM 4830 CA PRO C 88 49.510 36.797 2.556 1.00 34.10 C ATOM 4831 C PRO C 88 50.712 35.832 2.616 1.00 35.89 C ATOM 4832 O PRO C 88 51.703 36.153 3.279 1.00 37.77 O ATOM 4833 CB PRO C 88 48.204 36.104 2.961 1.00 26.29 C ATOM 4834 CG PRO C 88 47.157 36.935 2.312 1.00 25.36 C ATOM 4835 CD PRO C 88 47.746 37.441 1.008 1.00 33.04 C ATOM 4836 N PHE C 89 50.639 34.679 1.956 1.00 27.82 N ATOM 4837 CA PHE C 89 51.774 33.761 1.963 1.00 31.54 C ATOM 4838 C PHE C 89 53.009 34.405 1.306 1.00 36.57 C ATOM 4839 O PHE C 89 54.147 34.142 1.696 1.00 28.08 O ATOM 4840 CB PHE C 89 51.457 32.500 1.177 1.00 30.17 C ATOM 4841 CG PHE C 89 50.517 31.560 1.846 1.00 26.29 C ATOM 4842 CD1 PHE C 89 50.986 30.382 2.410 1.00 30.97 C ATOM 4843 CD2 PHE C 89 49.152 31.806 1.844 1.00 32.53 C ATOM 4844 CE1 PHE C 89 50.116 29.468 2.992 1.00 33.06 C ATOM 4845 CE2 PHE C 89 48.265 30.908 2.432 1.00 28.69 C ATOM 4846 CZ PHE C 89 48.749 29.735 3.006 1.00 37.87 C ATOM 4847 N GLY C 90 52.776 35.215 0.277 1.00 32.49 N ATOM 4848 CA GLY C 90 53.859 35.851 −0.452 1.00 29.73 C ATOM 4849 C GLY C 90 54.607 36.855 0.403 1.00 35.22 C ATOM 4850 O GLY C 90 55.810 37.064 0.246 1.00 24.87 O ATOM 4851 N ALA C 91 53.879 37.480 1.321 1.00 40.02 N ATOM 4852 CA ALA C 91 54.471 38.396 2.284 1.00 39.53 C ATOM 4853 C ALA C 91 55.507 37.694 3.182 1.00 38.46 C ATOM 4854 O ALA C 91 56.635 38.170 3.325 1.00 32.75 O ATOM 4855 CB ALA C 91 53.387 39.023 3.115 1.00 33.11 C ATOM 4856 N THR C 92 55.120 36.565 3.778 1.00 27.51 N ATOM 4857 CA THR C 92 56.030 35.791 4.619 1.00 24.40 C ATOM 4858 C THR C 92 57.316 35.479 3.874 1.00 30.89 C ATOM 4859 O THR C 92 58.406 35.605 4.419 1.00 33.79 O ATOM 4860 CB THR C 92 55.390 34.470 5.150 1.00 34.13 C ATOM 4861 OG1 THR C 92 55.414 33.451 4.138 1.00 30.20 O ATOM 4862 CG2 THR C 92 53.958 34.705 5.609 1.00 28.27 C ATOM 4863 N LEU C 93 57.186 35.085 2.616 1.00 34.44 N ATOM 4864 CA LEU C 93 58.345 34.768 1.798 1.00 36.58 C ATOM 4865 C LEU C 93 59.289 35.959 1.632 1.00 35.22 C ATOM 4866 O LEU C 93 60.508 35.791 1.577 1.00 39.31 O ATOM 4867 CB LEU C 93 57.896 34.253 0.428 1.00 33.49 C ATOM 4868 CG LEU C 93 58.936 33.740 −0.567 1.00 25.62 C ATOM 4869 CD1 LEU C 93 59.892 32.752 0.077 1.00 17.54 C ATOM 4870 CD2 LEU C 93 58.187 33.083 −1.707 1.00 31.92 C ATOM 4871 N VAL C 94 58.734 37.160 1.539 1.00 34.62 N ATOM 4872 CA VAL C 94 59.571 38.326 1.286 1.00 42.64 C ATOM 4873 C VAL C 94 60.167 38.872 2.578 1.00 52.48 C ATOM 4874 O VAL C 94 61.295 39.368 2.592 1.00 54.70 O ATOM 4875 CB VAL C 94 58.810 39.437 0.546 1.00 45.58 C ATOM 4876 CG1 VAL C 94 59.800 40.426 −0.058 1.00 37.70 C ATOM 4877 CG2 VAL C 94 57.938 38.837 −0.544 1.00 51.12 C ATOM 4878 N VAL C 95 59.411 38.772 3.663 1.00 40.50 N ATOM 4879 CA VAL C 95 59.899 39.196 4.965 1.00 43.07 C ATOM 4880 C VAL C 95 60.987 38.261 5.531 1.00 49.48 C ATOM 4881 O VAL C 95 61.956 38.722 6.134 1.00 54.37 O ATOM 4882 CB VAL C 95 58.741 39.334 5.974 1.00 40.04 C ATOM 4883 CG1 VAL C 95 59.275 39.663 7.349 1.00 58.24 C ATOM 4884 CG2 VAL C 95 57.765 40.404 5.513 1.00 51.46 C ATOM 4885 N ARG C 96 60.837 36.955 5.329 1.00 42.34 N ATOM 4886 CA ARG C 96 61.740 35.994 5.946 1.00 33.41 C ATOM 4887 C ARG C 96 62.779 35.404 5.014 1.00 33.06 C ATOM 4888 O ARG C 96 63.718 34.753 5.464 1.00 46.69 O ATOM 4889 CB ARG C 96 60.952 34.865 6.610 1.00 34.33 C ATOM 4890 CG ARG C 96 60.418 35.226 7.996 1.00 55.49 C ATOM 4891 CD ARG C 96 61.555 35.460 9.000 1.00 45.07 C ATOM 4892 NE ARG C 96 62.372 34.266 9.198 1.00 37.37 N ATOM 4893 CZ ARG C 96 61.968 33.193 9.876 1.00 43.85 C ATOM 4894 NH1 ARG C 96 60.754 33.167 10.419 1.00 28.51 N ATOM 4895 NH2 ARG C 96 62.778 32.143 10.008 1.00 37.06 N ATOM 4896 N GLY C 97 62.614 35.618 3.721 1.00 33.08 N ATOM 4897 CA GLY C 97 63.492 35.001 2.739 1.00 27.90 C ATOM 4898 C GLY C 97 63.513 33.477 2.778 1.00 32.65 C ATOM 4899 O GLY C 97 64.519 32.866 2.436 1.00 45.61 O ATOM 4900 N THR C 98 62.414 32.858 3.201 1.00 29.36 N ATOM 4901 CA THR C 98 62.305 31.397 3.234 1.00 29.74 C ATOM 4902 C THR C 98 60.838 31.043 3.157 1.00 35.04 C ATOM 4903 O THR C 98 59.973 31.905 3.372 1.00 31.10 O ATOM 4904 CB THR C 98 62.823 30.770 4.555 1.00 27.89 C ATOM 4905 OG1 THR C 98 63.751 31.651 5.184 1.00 40.33 O ATOM 4906 CG2 THR C 98 63.471 29.419 4.301 1.00 23.25 C ATOM 4907 N TRP C 99 60.565 29.770 2.881 1.00 20.88 N ATOM 4908 CA TRP C 99 59.207 29.275 2.856 1.00 19.61 C ATOM 4909 C TRP C 99 58.918 28.485 4.128 1.00 24.95 C ATOM 4910 O TRP C 99 59.577 27.484 4.411 1.00 24.39 O ATOM 4911 CB TRP C 99 58.977 28.426 1.612 1.00 20.24 C ATOM 4912 CG TRP C 99 57.543 28.104 1.366 1.00 22.90 C ATOM 4913 CD1 TRP C 99 56.952 26.890 1.494 1.00 20.90 C ATOM 4914 CD2 TRP C 99 56.511 29.016 0.963 1.00 19.43 C ATOM 4915 NE1 TRP C 99 55.618 26.978 1.177 1.00 26.28 N ATOM 4916 CE2 TRP C 99 55.322 28.274 0.847 1.00 23.08 C ATOM 4917 CE3 TRP C 99 56.480 30.384 0.680 1.00 19.54 C ATOM 4918 CZ2 TRP C 99 54.113 28.852 0.471 1.00 18.38 C ATOM 4919 CZ3 TRP C 99 55.278 30.954 0.299 1.00 21.30 C ATOM 4920 CH2 TRP C 99 54.112 30.188 0.203 1.00 21.48 C ATOM 4921 N LEU C 100 57.932 28.942 4.897 1.00 24.19 N ATOM 4922 CA LEU C 100 57.631 28.327 6.191 1.00 26.92 C ATOM 4923 C LEU C 100 56.611 27.203 6.094 1.00 28.16 C ATOM 4924 O LEU C 100 56.377 26.488 7.070 1.00 28.87 O ATOM 4925 CB LEU C 100 57.082 29.354 7.196 1.00 28.77 C ATOM 4926 CG LEU C 100 57.759 30.644 7.683 1.00 33.42 C ATOM 4927 CD1 LEU C 100 57.096 31.022 8.992 1.00 32.17 C ATOM 4928 CD2 LEU C 100 59.267 30.523 7.876 1.00 30.34 C ATOM 4929 N TRP C 101 55.999 27.041 4.927 1.00 28.57 N ATOM 4930 CA TRP C 101 54.730 26.323 4.871 1.00 24.65 C ATOM 4931 C TRP C 101 54.765 24.930 4.233 1.00 25.38 C ATOM 4932 O TRP C 101 53.751 24.247 4.198 1.00 32.27 O ATOM 4933 CB TRP C 101 53.664 27.224 4.247 1.00 19.60 C ATOM 4934 CG TRP C 101 53.709 28.615 4.819 1.00 24.28 C ATOM 4935 CD1 TRP C 101 54.181 29.744 4.204 1.00 26.56 C ATOM 4936 CD2 TRP C 101 53.311 29.021 6.135 1.00 25.10 C ATOM 4937 NE1 TRP C 101 54.085 30.832 5.052 1.00 23.63 N ATOM 4938 CE2 TRP C 101 53.553 30.413 6.241 1.00 25.25 C ATOM 4939 CE3 TRP C 101 52.756 28.349 7.226 1.00 24.58 C ATOM 4940 CZ2 TRP C 101 53.257 31.138 7.393 1.00 21.63 C ATOM 4941 CZ3 TRP C 101 52.463 29.073 8.375 1.00 21.42 C ATOM 4942 CH2 TRP C 101 52.718 30.453 8.446 1.00 23.63 C ATOM 4943 N GLY C 102 55.925 24.497 3.751 1.00 30.89 N ATOM 4944 CA GLY C 102 56.064 23.138 3.252 1.00 24.52 C ATOM 4945 C GLY C 102 56.036 22.988 1.742 1.00 27.25 C ATOM 4946 O GLY C 102 55.484 23.817 1.023 1.00 28.32 O ATOM 4947 N SER C 103 56.626 21.908 1.250 1.00 27.87 N ATOM 4948 CA SER C 103 56.721 21.706 −0.193 1.00 23.71 C ATOM 4949 C SER C 103 55.348 21.701 −0.863 1.00 28.14 C ATOM 4950 O SER C 103 55.159 22.326 −1.901 1.00 28.86 O ATOM 4951 CB SER C 103 57.488 20.422 −0.523 1.00 23.74 C ATOM 4952 OG SER C 103 58.771 20.426 0.088 1.00 41.82 O ATOM 4953 N PHE C 104 54.382 21.007 −0.273 1.00 24.10 N ATOM 4954 CA PHE C 104 53.090 20.900 −0.926 1.00 23.87 C ATOM 4955 C PHE C 104 52.397 22.245 −1.055 1.00 26.73 C ATOM 4956 O PHE C 104 51.870 22.571 −2.116 1.00 30.36 O ATOM 4957 CB PHE C 104 52.170 19.910 −0.226 1.00 26.53 C ATOM 4958 CG PHE C 104 50.777 19.926 −0.758 1.00 24.89 C ATOM 4959 CD1 PHE C 104 50.519 19.500 −2.054 1.00 27.85 C ATOM 4960 CD2 PHE C 104 49.729 20.385 0.016 1.00 28.88 C ATOM 4961 CE1 PHE C 104 49.241 19.511 −2.563 1.00 20.54 C ATOM 4962 CE2 PHE C 104 48.441 20.403 −0.489 1.00 36.85 C ATOM 4963 CZ PHE C 104 48.200 19.965 −1.784 1.00 31.30 C ATOM 4964 N LEU C 105 52.383 23.021 0.023 1.00 30.21 N ATOM 4965 CA LEU C 105 51.724 24.323 −0.019 1.00 24.99 C ATOM 4966 C LEU C 105 52.474 25.273 −0.931 1.00 25.78 C ATOM 4967 O LEU C 105 51.877 26.213 −1.463 1.00 22.68 O ATOM 4968 CB LEU C 105 51.572 24.945 1.372 1.00 27.03 C ATOM 4969 CG LEU C 105 50.452 24.467 2.310 1.00 30.97 C ATOM 4970 CD1 LEU C 105 50.056 25.593 3.279 1.00 21.34 C ATOM 4971 CD2 LEU C 105 49.248 23.993 1.527 1.00 27.82 C ATOM 4972 N CYS C 106 53.777 25.031 −1.116 1.00 24.65 N ATOM 4973 CA CYS C 106 54.573 25.853 −2.028 1.00 22.14 C ATOM 4974 C CYS C 106 54.015 25.740 −3.441 1.00 27.53 C ATOM 4975 O CYS C 106 53.745 26.752 −4.103 1.00 22.83 O ATOM 4976 CB CYS C 106 56.039 25.438 −2.019 1.00 23.24 C ATOM 4977 SG CYS C 106 57.079 26.373 −3.178 1.00 26.49 S ATOM 4978 N GLU C 107 53.829 24.499 −3.887 1.00 26.12 N ATOM 4979 CA GLU C 107 53.316 24.234 −5.222 1.00 22.41 C ATOM 4980 C GLU C 107 51.913 24.753 −5.362 1.00 23.24 C ATOM 4981 O GLU C 107 51.614 25.458 −6.315 1.00 22.18 O ATOM 4982 CB GLU C 107 53.373 22.747 −5.553 1.00 31.93 C ATOM 4983 CG GLU C 107 54.483 22.401 −6.531 1.00 52.80 C ATOM 4984 CD GLU C 107 54.404 20.972 −7.037 1.00 72.07 C ATOM 4985 OE1 GLU C 107 54.906 20.708 −8.164 1.00 61.95 O ATOM 4986 OE2 GLU C 107 53.837 20.125 −6.305 1.00 66.39 O ATOM 4987 N LEU C 108 51.063 24.417 −4.395 1.00 22.35 N ATOM 4988 CA LEU C 108 49.693 24.909 −4.364 1.00 25.20 C ATOM 4989 C LEU C 108 49.607 26.431 −4.464 1.00 26.48 C ATOM 4990 O LEU C 108 48.812 26.965 −5.244 1.00 28.90 O ATOM 4991 CB LEU C 108 48.970 24.443 −3.111 1.00 23.53 C ATOM 4992 CG LEU C 108 47.459 24.629 −3.237 1.00 23.55 C ATOM 4993 CD1 LEU C 108 46.966 23.705 −4.334 1.00 25.56 C ATOM 4994 CD2 LEU C 108 46.745 24.349 −1.911 1.00 22.23 C ATOM 4995 N TRP C 109 50.420 27.120 −3.670 1.00 25.27 N ATOM 4996 CA TRP C 109 50.461 28.579 −3.673 1.00 21.16 C ATOM 4997 C TRP C 109 50.813 29.090 −5.060 1.00 25.82 C ATOM 4998 O TRP C 109 50.160 29.990 −5.574 1.00 25.91 O ATOM 4999 CB TRP C 109 51.480 29.084 −2.637 1.00 21.91 C ATOM 5000 CG TRP C 109 51.818 30.550 −2.748 1.00 20.09 C ATOM 5001 CD1 TRP C 109 50.986 31.596 −2.516 1.00 23.45 C ATOM 5002 CD2 TRP C 109 53.080 31.119 −3.117 1.00 18.35 C ATOM 5003 NE1 TRP C 109 51.641 32.783 −2.720 1.00 19.96 N ATOM 5004 CE2 TRP C 109 52.930 32.519 −3.089 1.00 20.06 C ATOM 5005 CE3 TRP C 109 54.325 30.580 −3.462 1.00 23.18 C ATOM 5006 CZ2 TRP C 109 53.976 33.393 −3.401 1.00 22.55 C ATOM 5007 CZ3 TRP C 109 55.363 31.448 −3.773 1.00 24.24 C ATOM 5008 CH2 TRP C 109 55.180 32.839 −3.746 1.00 23.16 C ATOM 5009 N THR C 110 51.856 28.508 −5.653 1.00 26.48 N ATOM 5010 CA THR C 110 52.337 28.898 −6.979 1.00 23.25 C ATOM 5011 C THR C 110 51.251 28.707 −8.040 1.00 24.03 C ATOM 5012 O THR C 110 50.966 29.623 −8.802 1.00 25.42 O ATOM 5013 CB THR C 110 53.614 28.111 −7.355 1.00 24.26 C ATOM 5014 OG1 THR C 110 54.665 28.456 −6.449 1.00 28.58 O ATOM 5015 CG2 THR C 110 54.068 28.416 −8.777 1.00 16.00 C ATOM 5016 N SER C 111 50.646 27.520 −8.080 1.00 24.74 N ATOM 5017 CA SER C 111 49.447 27.274 −8.895 1.00 27.42 C ATOM 5018 C SER C 111 48.401 28.400 −8.818 1.00 30.00 C ATOM 5019 O SER C 111 47.906 28.860 −9.849 1.00 19.45 O ATOM 5020 CB SER C 111 48.779 25.963 −8.472 1.00 26.85 C ATOM 5021 OG SER C 111 49.579 24.844 −8.813 1.00 34.61 O ATOM 5022 N LEU C 112 48.076 28.825 −7.593 1.00 19.84 N ATOM 5023 CA LEU C 112 47.065 29.853 −7.337 1.00 20.69 C ATOM 5024 C LEU C 112 47.414 31.214 −7.888 1.00 24.15 C ATOM 5025 O LEU C 112 46.567 31.937 −8.410 1.00 25.01 O ATOM 5026 CB LEU C 112 46.857 30.026 −5.844 1.00 21.92 C ATOM 5027 CG LEU C 112 45.726 29.181 −5.303 1.00 33.90 C ATOM 5028 CD1 LEU C 112 45.388 29.675 −3.907 1.00 28.59 C ATOM 5029 CD2 LEU C 112 44.534 29.276 −6.261 1.00 22.69 C ATOM 5030 N ASP C 113 48.673 31.568 −7.725 1.00 20.05 N ATOM 5031 CA ASP C 113 49.187 32.836 −8.163 1.00 25.36 C ATOM 5032 C ASP C 113 48.993 32.979 −9.672 1.00 27.63 C ATOM 5033 O ASP C 113 48.466 33.983 −10.155 1.00 30.60 O ATOM 5034 CB ASP C 113 50.667 32.862 −7.807 1.00 30.35 C ATOM 5035 CG ASP C 113 51.303 34.195 −8.045 1.00 32.92 C ATOM 5036 OD1 ASP C 113 50.765 34.997 −8.840 1.00 33.21 O ATOM 5037 OD2 ASP C 113 52.361 34.427 −7.428 1.00 33.30 O ATOM 5038 N VAL C 114 49.417 31.948 −10.394 1.00 21.77 N ATOM 5039 CA VAL C 114 49.391 31.903 −11.844 1.00 23.57 C ATOM 5040 C VAL C 114 47.965 31.859 −12.395 1.00 26.37 C ATOM 5041 O VAL C 114 47.630 32.558 −13.365 1.00 23.16 O ATOM 5042 CB VAL C 114 50.212 30.686 −12.348 1.00 29.30 C ATOM 5043 CG1 VAL C 114 50.087 30.508 −13.839 1.00 24.31 C ATOM 5044 CG2 VAL C 114 51.673 30.865 −11.984 1.00 26.91 C ATOM 5045 N LEU C 115 47.127 31.039 −11.770 1.00 25.73 N ATOM 5046 CA LEU C 115 45.706 30.987 −12.100 1.00 18.78 C ATOM 5047 C LEU C 115 45.057 32.366 −12.050 1.00 22.53 C ATOM 5048 O LEU C 115 44.332 32.749 −12.971 1.00 24.52 O ATOM 5049 CB LEU C 115 44.977 30.039 −11.160 1.00 16.64 C ATOM 5050 CG LEU C 115 43.489 29.887 −11.435 1.00 23.31 C ATOM 5051 CD1 LEU C 115 43.260 29.559 −12.896 1.00 25.28 C ATOM 5052 CD2 LEU C 115 42.917 28.808 −10.557 1.00 21.26 C ATOM 5053 N CYS C 116 45.328 33.118 −10.984 1.00 24.03 N ATOM 5054 CA CYS C 116 44.710 34.433 −10.813 1.00 28.63 C ATOM 5055 C CYS C 116 45.114 35.457 −11.878 1.00 30.89 C ATOM 5056 O CYS C 116 44.287 36.268 −12.298 1.00 29.82 O ATOM 5057 CB CYS C 116 44.930 34.982 −9.406 1.00 19.38 C ATOM 5058 SG CYS C 116 43.944 34.146 −8.150 1.00 45.74 S ATOM 5059 N VAL C 117 46.368 35.423 −12.322 1.00 25.78 N ATOM 5060 CA VAL C 117 46.810 36.353 −13.365 1.00 29.93 C ATOM 5061 C VAL C 117 46.317 35.921 −14.752 1.00 31.70 C ATOM 5062 O VAL C 117 45.958 36.759 −15.574 1.00 22.36 O ATOM 5063 CB VAL C 117 48.342 36.534 −13.383 1.00 29.38 C ATOM 5064 CG1 VAL C 117 48.722 37.707 −14.283 1.00 30.30 C ATOM 5065 CG2 VAL C 117 48.854 36.759 −11.979 1.00 24.88 C ATOM 5066 N THR C 118 46.288 34.614 −15.008 1.00 32.57 N ATOM 5067 CA THR C 118 45.751 34.112 −16.270 1.00 27.99 C ATOM 5068 C THR C 118 44.279 34.493 −16.403 1.00 30.35 C ATOM 5069 O THR C 118 43.859 35.008 −17.453 1.00 22.53 O ATOM 5070 CB THR C 118 45.887 32.579 −16.401 1.00 30.37 C ATOM 5071 OG1 THR C 118 47.271 32.208 −16.363 1.00 27.91 O ATOM 5072 CG2 THR C 118 45.276 32.093 −17.706 1.00 22.03 C ATOM 5073 N ALA C 119 43.503 34.248 −15.343 1.00 20.70 N ATOM 5074 CA ALA C 119 42.069 34.531 −15.377 1.00 22.88 C ATOM 5075 C ALA C 119 41.728 36.025 −15.522 1.00 24.49 C ATOM 5076 O ALA C 119 40.722 36.377 −16.135 1.00 27.90 O ATOM 5077 CB ALA C 119 41.353 33.907 −14.177 1.00 22.79 C ATOM 5078 N SER C 120 42.567 36.897 −14.977 1.00 28.58 N ATOM 5079 CA SER C 120 42.356 38.335 −15.106 1.00 30.17 C ATOM 5080 C SER C 120 42.446 38.771 −16.558 1.00 30.24 C ATOM 5081 O SER C 120 41.458 39.250 −17.119 1.00 31.14 O ATOM 5082 CB SER C 120 43.374 39.127 −14.283 1.00 28.09 C ATOM 5083 OG SER C 120 43.176 38.937 −12.893 1.00 39.21 O ATOM 5084 N ILE C 121 43.629 38.610 −17.155 1.00 23.05 N ATOM 5085 CA ILE C 121 43.855 39.011 −18.539 1.00 23.20 C ATOM 5086 C ILE C 121 42.824 38.335 −19.443 1.00 24.90 C ATOM 5087 O ILE C 121 42.269 38.962 −20.342 1.00 30.34 O ATOM 5088 CB ILE C 121 45.315 38.736 −19.009 1.00 22.40 C ATOM 5089 CG1 ILE C 121 45.663 39.537 −20.267 1.00 24.10 C ATOM 5090 CG2 ILE C 121 45.541 37.262 −19.283 1.00 22.46 C ATOM 5091 CD1 ILE C 121 45.255 40.976 −20.211 1.00 31.26 C ATOM 5092 N GLU C 122 42.534 37.067 −19.185 1.00 27.17 N ATOM 5093 CA GLU C 122 41.527 36.369 −19.980 1.00 28.10 C ATOM 5094 C GLU C 122 40.176 37.048 −19.865 1.00 29.87 C ATOM 5095 O GLU C 122 39.465 37.176 −20.856 1.00 32.92 O ATOM 5096 CB GLU C 122 41.409 34.897 −19.581 1.00 25.66 C ATOM 5097 CG GLU C 122 42.333 33.969 −20.342 1.00 27.36 C ATOM 5098 CD GLU C 122 42.033 32.497 −20.078 1.00 43.44 C ATOM 5099 OE1 GLU C 122 40.943 32.195 −19.535 1.00 42.49 O ATOM 5100 OE2 GLU C 122 42.884 31.640 −20.417 1.00 43.62 O ATOM 5101 N THR C 123 39.820 37.477 −18.658 1.00 31.11 N ATOM 5102 CA THR C 123 38.556 38.174 −18.445 1.00 27.09 C ATOM 5103 C THR C 123 38.561 39.557 −19.091 1.00 30.79 C ATOM 5104 O THR C 123 37.600 39.945 −19.731 1.00 31.71 O ATOM 5105 CB THR C 123 38.217 38.294 −16.952 1.00 32.70 C ATOM 5106 OG1 THR C 123 37.853 37.004 −16.442 1.00 34.25 O ATOM 5107 CG2 THR C 123 37.063 39.260 −16.734 1.00 30.31 C ATOM 5108 N LEU C 124 39.649 40.297 −18.935 1.00 30.24 N ATOM 5109 CA LEU C 124 39.759 41.592 −19.581 1.00 29.95 C ATOM 5110 C LEU C 124 39.564 41.447 −21.082 1.00 35.53 C ATOM 5111 O LEU C 124 39.079 42.352 −21.752 1.00 44.29 O ATOM 5112 CB LEU C 124 41.113 42.228 −19.275 1.00 33.34 C ATOM 5113 CG LEU C 124 41.166 42.798 −17.858 1.00 28.66 C ATOM 5114 CD1 LEU C 124 42.592 43.183 −17.449 1.00 31.00 C ATOM 5115 CD2 LEU C 124 40.240 43.977 −17.774 1.00 31.04 C ATOM 5116 N CYS C 125 39.940 40.294 −21.609 1.00 35.81 N ATOM 5117 CA CYS C 125 39.780 40.030 −23.024 1.00 36.50 C ATOM 5118 C CYS C 125 38.296 39.991 −23.338 1.00 36.65 C ATOM 5119 O CYS C 125 37.795 40.736 −24.186 1.00 39.03 O ATOM 5120 CB CYS C 125 40.415 38.688 −23.370 1.00 35.76 C ATOM 5121 SG CYS C 125 41.535 38.785 −24.745 1.00 47.66 S ATOM 5122 N VAL C 126 37.592 39.116 −22.636 1.00 33.56 N ATOM 5123 CA VAL C 126 36.158 38.986 −22.808 1.00 29.67 C ATOM 5124 C VAL C 126 35.449 40.340 −22.703 1.00 33.19 C ATOM 5125 O VAL C 126 34.646 40.676 −23.564 1.00 40.38 O ATOM 5126 CB VAL C 126 35.578 37.948 −21.832 1.00 31.47 C ATOM 5127 CG1 VAL C 126 34.050 38.045 −21.757 1.00 34.32 C ATOM 5128 CG2 VAL C 126 36.009 36.557 −22.254 1.00 24.96 C ATOM 5129 N ILE C 127 35.762 41.123 −21.673 1.00 31.75 N ATOM 5130 CA ILE C 127 35.217 42.481 −21.532 1.00 34.41 C ATOM 5131 C ILE C 127 35.368 43.301 −22.817 1.00 39.24 C ATOM 5132 O ILE C 127 34.425 43.952 −23.257 1.00 39.02 O ATOM 5133 CB ILE C 127 35.892 43.267 −20.376 1.00 45.70 C ATOM 5134 CG1 ILE C 127 35.440 42.751 −19.013 1.00 32.84 C ATOM 5135 CG2 ILE C 127 35.603 44.767 −20.472 1.00 35.85 C ATOM 5136 CD1 ILE C 127 36.264 43.337 −17.884 1.00 37.36 C ATOM 5137 N ALA C 128 36.552 43.270 −23.419 1.00 33.41 N ATOM 5138 CA ALA C 128 36.794 44.048 −24.626 1.00 36.54 C ATOM 5139 C ALA C 128 35.979 43.534 −25.816 1.00 44.44 C ATOM 5140 O ALA C 128 35.289 44.310 −26.490 1.00 49.06 O ATOM 5141 CB ALA C 128 38.283 44.081 −24.961 1.00 38.07 C ATOM 5142 N ILE C 129 36.070 42.229 −26.069 1.00 33.39 N ATOM 5143 CA ILE C 129 35.333 41.598 −27.159 1.00 36.73 C ATOM 5144 C ILE C 129 33.817 41.783 −27.029 1.00 39.32 C ATOM 5145 O ILE C 129 33.112 41.914 −28.027 1.00 35.89 O ATOM 5146 CB ILE C 129 35.628 40.094 −27.219 1.00 41.68 C ATOM 5147 CG1 ILE C 129 37.066 39.855 −27.673 1.00 39.85 C ATOM 5148 CG2 ILE C 129 34.630 39.387 −28.138 1.00 33.75 C ATOM 5149 CD1 ILE C 129 37.490 38.410 −27.582 1.00 28.06 C ATOM 5150 N ASP C 130 33.330 41.773 −25.790 1.00 40.86 N ATOM 5151 CA ASP C 130 31.919 41.969 −25.485 1.00 37.27 C ATOM 5152 C ASP C 130 31.480 43.369 −25.890 1.00 40.65 C ATOM 5153 O ASP C 130 30.484 43.539 −26.588 1.00 38.96 O ATOM 5154 CB ASP C 130 31.688 41.747 −23.985 1.00 42.29 C ATOM 5155 CG ASP C 130 30.522 42.570 −23.425 1.00 56.32 C ATOM 5156 OD1 ASP C 130 29.377 42.359 −23.873 1.00 66.96 O ATOM 5157 OD2 ASP C 130 30.749 43.408 −22.516 1.00 53.17 O ATOM 5158 N ARG C 131 32.234 44.364 −25.438 1.00 42.60 N ATOM 5159 CA ARG C 131 31.996 45.752 −25.801 1.00 48.66 C ATOM 5160 C ARG C 131 32.043 45.940 −27.310 1.00 42.20 C ATOM 5161 O ARG C 131 31.173 46.591 −27.891 1.00 40.78 O ATOM 5162 CB ARG C 131 33.028 46.665 −25.133 1.00 47.37 C ATOM 5163 CG ARG C 131 32.807 46.863 −23.639 1.00 40.25 C ATOM 5164 CD ARG C 131 31.416 47.389 −23.349 1.00 37.07 C ATOM 5165 NE ARG C 131 30.418 46.328 −23.276 1.00 50.00 N ATOM 5166 CZ ARG C 131 29.106 46.544 −23.196 1.00 59.17 C ATOM 5167 NH1 ARG C 131 28.635 47.787 −23.195 1.00 56.73 N ATOM 5168 NH2 ARG C 131 28.261 45.519 −23.127 1.00 44.45 N ATOM 5169 N TYR C 132 33.058 45.367 −27.942 1.00 36.06 N ATOM 5170 CA TYR C 132 33.188 45.492 −29.389 1.00 50.69 C ATOM 5171 C TYR C 132 32.004 44.899 −30.159 1.00 51.94 C ATOM 5172 O TYR C 132 31.674 45.366 −31.250 1.00 53.20 O ATOM 5173 CB TYR C 132 34.492 44.878 −29.889 1.00 44.59 C ATOM 5174 CG TYR C 132 34.580 44.883 −31.391 1.00 43.69 C ATOM 5175 CD1 TYR C 132 35.074 45.986 −32.074 1.00 52.80 C ATOM 5176 CD2 TYR C 132 34.148 43.790 −32.129 1.00 50.07 C ATOM 5177 CE1 TYR C 132 35.147 45.996 −33.446 1.00 56.18 C ATOM 5178 CE2 TYR C 132 34.218 43.788 −33.496 1.00 56.67 C ATOM 5179 CZ TYR C 132 34.713 44.893 −34.154 1.00 61.49 C ATOM 5180 OH TYR C 132 34.772 44.884 −35.527 1.00 68.89 O ATOM 5181 N LEU C 133 31.379 43.866 −29.606 1.00 39.89 N ATOM 5182 CA LEU C 133 30.176 43.309 −30.216 1.00 43.18 C ATOM 5183 C LEU C 133 28.948 44.184 −29.936 1.00 46.36 C ATOM 5184 O LEU C 133 28.126 44.412 −30.821 1.00 46.64 O ATOM 5185 CB LEU C 133 29.920 41.880 −29.737 1.00 33.56 C ATOM 5186 CG LEU C 133 30.940 40.798 −30.106 1.00 41.93 C ATOM 5187 CD1 LEU C 133 30.559 39.491 −29.400 1.00 33.81 C ATOM 5188 CD2 LEU C 133 31.078 40.593 −31.621 1.00 28.13 C ATOM 5189 N ALA C 134 28.823 44.669 −28.706 1.00 46.69 N ATOM 5190 CA ALA C 134 27.684 45.494 −28.342 1.00 42.61 C ATOM 5191 C ALA C 134 27.689 46.743 −29.199 1.00 43.95 C ATOM 5192 O ALA C 134 26.649 47.192 −29.671 1.00 54.21 O ATOM 5193 CB ALA C 134 27.730 45.857 −26.873 1.00 29.76 C ATOM 5194 N ILE C 135 28.874 47.282 −29.428 1.00 50.79 N ATOM 5195 CA ILE C 135 29.001 48.541 −30.143 1.00 55.92 C ATOM 5196 C ILE C 135 28.780 48.403 −31.659 1.00 55.52 C ATOM 5197 O ILE C 135 28.214 49.302 −32.277 1.00 63.61 O ATOM 5198 CB ILE C 135 30.359 49.202 −29.861 1.00 58.21 C ATOM 5199 CG1 ILE C 135 30.169 50.635 −29.380 1.00 51.90 C ATOM 5200 CG2 ILE C 135 31.260 49.147 −31.085 1.00 63.93 C ATOM 5201 CD1 ILE C 135 31.483 51.349 −29.136 1.00 66.88 C ATOM 5202 N THR C 136 29.206 47.287 −32.254 1.00 52.09 N ATOM 5203 CA THR C 136 29.015 47.077 −33.697 1.00 46.61 C ATOM 5204 C THR C 136 27.734 46.322 −34.062 1.00 52.82 C ATOM 5205 O THR C 136 27.143 46.598 −35.102 1.00 61.96 O ATOM 5206 CB THR C 136 30.212 46.351 −34.381 1.00 51.99 C ATOM 5207 OG1 THR C 136 30.191 44.952 −34.056 1.00 45.16 O ATOM 5208 CG2 THR C 136 31.558 46.982 −33.998 1.00 45.18 C ATOM 5209 N SER C 137 27.302 45.377 −33.227 1.00 52.87 N ATOM 5210 CA SER C 137 26.137 44.541 −33.556 1.00 49.57 C ATOM 5211 C SER C 137 24.981 44.611 −32.559 1.00 51.96 C ATOM 5212 O SER C 137 24.434 43.578 −32.183 1.00 51.48 O ATOM 5213 CB SER C 137 26.556 43.077 −33.700 1.00 41.53 C ATOM 5214 OG SER C 137 27.431 42.899 −34.796 1.00 62.51 O ATOM 5215 N PRO C 138 24.585 45.824 −32.150 1.00 55.98 N ATOM 5216 CA PRO C 138 23.587 46.003 −31.086 1.00 53.71 C ATOM 5217 C PRO C 138 22.386 45.055 −31.156 1.00 60.77 C ATOM 5218 O PRO C 138 21.975 44.556 −30.112 1.00 65.02 O ATOM 5219 CB PRO C 138 23.133 47.459 −31.275 1.00 39.21 C ATOM 5220 CG PRO C 138 23.695 47.868 −32.625 1.00 61.71 C ATOM 5221 CD PRO C 138 24.974 47.121 −32.720 1.00 45.27 C ATOM 5222 N PHE C 139 21.831 44.813 −32.341 1.00 62.93 N ATOM 5223 CA PHE C 139 20.649 43.954 −32.448 1.00 64.31 C ATOM 5224 C PHE C 139 20.987 42.477 −32.279 1.00 64.55 C ATOM 5225 O PHE C 139 20.323 41.765 −31.519 1.00 69.43 O ATOM 5226 CB PHE C 139 19.897 44.177 −33.768 1.00 83.98 C ATOM 5227 CG PHE C 139 18.618 43.382 −33.879 1.00 95.82 C ATOM 5228 CD1 PHE C 139 17.420 43.891 −33.391 1.00 94.78 C ATOM 5229 CD2 PHE C 139 18.615 42.120 −34.462 1.00 89.49 C ATOM 5230 CE1 PHE C 139 16.245 43.159 −33.484 1.00 85.31 C ATOM 5231 CE2 PHE C 139 17.442 41.382 −34.554 1.00 85.42 C ATOM 5232 CZ PHE C 139 16.258 41.904 −34.064 1.00 82.57 C ATOM 5233 N ARG C 140 22.012 42.011 −32.989 1.00 60.87 N ATOM 5234 CA ARG C 140 22.449 40.625 −32.842 1.00 60.29 C ATOM 5235 C ARG C 140 23.063 40.364 −31.468 1.00 61.68 C ATOM 5236 O ARG C 140 23.251 39.215 −31.074 1.00 69.06 O ATOM 5237 CB ARG C 140 23.425 40.231 −33.945 1.00 55.75 C ATOM 5238 CG ARG C 140 22.756 39.948 −35.273 1.00 62.53 C ATOM 5239 CD ARG C 140 23.746 39.389 −36.272 1.00 70.85 C ATOM 5240 NE ARG C 140 23.082 38.920 −37.482 1.00 85.03 N ATOM 5241 CZ ARG C 140 23.689 38.228 −38.440 1.00 90.43 C ATOM 5242 NH1 ARG C 140 24.974 37.929 −38.318 1.00 92.11 N ATOM 5243 NH2 ARG C 140 23.016 37.835 −39.517 1.00 84.82 N ATOM 5244 N TYR C 141 23.354 41.433 −30.734 1.00 58.53 N ATOM 5245 CA TYR C 141 23.923 41.308 −29.397 1.00 52.86 C ATOM 5246 C TYR C 141 22.867 41.074 −28.308 1.00 64.20 C ATOM 5247 O TYR C 141 22.998 40.142 −27.515 1.00 66.32 O ATOM 5248 CB TYR C 141 24.778 42.533 −29.067 1.00 54.37 C ATOM 5249 CG TYR C 141 25.363 42.517 −27.680 1.00 53.21 C ATOM 5250 CD1 TYR C 141 26.575 41.886 −27.418 1.00 62.39 C ATOM 5251 CD2 TYR C 141 24.701 43.132 −26.626 1.00 65.34 C ATOM 5252 CE1 TYR C 141 27.112 41.869 −26.137 1.00 58.10 C ATOM 5253 CE2 TYR C 141 25.226 43.123 −25.347 1.00 64.84 C ATOM 5254 CZ TYR C 141 26.428 42.493 −25.107 1.00 60.66 C ATOM 5255 OH TYR C 141 26.932 42.495 −23.825 1.00 63.54 O ATOM 5256 N GLN C 142 21.831 41.913 −28.274 1.00 61.43 N ATOM 5257 CA GLN C 142 20.763 41.812 −27.273 1.00 67.69 C ATOM 5258 C GLN C 142 20.123 40.428 −27.183 1.00 73.75 C ATOM 5259 O GLN C 142 19.857 39.920 −26.086 1.00 72.00 O ATOM 5260 CB GLN C 142 19.655 42.819 −27.572 1.00 89.63 C ATOM 5261 CG GLN C 142 19.919 44.241 −27.131 1.00 100.22 C ATOM 5262 CD GLN C 142 18.805 45.180 −27.567 1.00 121.31 C ATOM 5263 OE1 GLN C 142 17.651 44.765 −27.733 1.00 98.60 O ATOM 5264 NE2 GLN C 142 19.147 46.450 −27.763 1.00 124.72 N ATOM 5265 N SER C 143 19.850 39.832 −28.341 1.00 75.52 N ATOM 5266 CA SER C 143 19.154 38.548 −28.395 1.00 74.63 C ATOM 5267 C SER C 143 20.040 37.391 −27.948 1.00 70.33 C ATOM 5268 O SER C 143 19.588 36.505 −27.219 1.00 76.73 O ATOM 5269 CB SER C 143 18.562 38.292 −29.792 1.00 78.24 C ATOM 5270 OG SER C 143 19.232 39.038 −30.798 1.00 69.78 O ATOM 5271 N LEU C 144 21.302 37.413 −28.365 1.00 58.65 N ATOM 5272 CA LEU C 144 22.230 36.341 −28.017 1.00 62.72 C ATOM 5273 C LEU C 144 22.778 36.420 −26.587 1.00 62.92 C ATOM 5274 O LEU C 144 22.989 35.398 −25.939 1.00 57.27 O ATOM 5275 CB LEU C 144 23.371 36.272 −29.034 1.00 56.96 C ATOM 5276 CG LEU C 144 22.823 35.930 −30.420 1.00 68.90 C ATOM 5277 CD1 LEU C 144 23.919 35.470 −31.367 1.00 48.42 C ATOM 5278 CD2 LEU C 144 21.741 34.864 −30.289 1.00 56.67 C ATOM 5279 N MET C 145 22.994 37.629 −26.086 1.00 55.61 N ATOM 5280 CA MET C 145 23.630 37.785 −24.781 1.00 58.58 C ATOM 5281 C MET C 145 22.669 38.017 −23.610 1.00 53.92 C ATOM 5282 O MET C 145 22.148 39.112 −23.432 1.00 54.95 O ATOM 5283 CB MET C 145 24.678 38.899 −24.838 1.00 56.51 C ATOM 5284 CG MET C 145 26.067 38.428 −25.269 1.00 69.80 C ATOM 5285 SD MET C 145 27.180 38.084 −23.874 1.00 81.42 S ATOM 5286 CE MET C 145 26.487 36.565 −23.218 1.00 54.05 C ATOM 5287 N THR C 146 22.441 36.972 −22.821 1.00 46.04 N ATOM 5288 CA THR C 146 21.707 37.094 −21.568 1.00 45.12 C ATOM 5289 C THR C 146 22.691 37.029 −20.394 1.00 51.33 C ATOM 5290 O THR C 146 23.903 37.029 −20.604 1.00 55.24 O ATOM 5291 CB THR C 146 20.622 35.998 −21.428 1.00 56.69 C ATOM 5292 OG1 THR C 146 21.231 34.698 −21.463 1.00 51.03 O ATOM 5293 CG2 THR C 146 19.604 36.110 −22.555 1.00 54.71 C ATOM 5294 N ARG C 147 22.180 36.978 −19.164 1.00 51.50 N ATOM 5295 CA ARG C 147 23.051 36.906 −17.989 1.00 41.33 C ATOM 5296 C ARG C 147 23.474 35.474 −17.678 1.00 44.42 C ATOM 5297 O ARG C 147 24.560 35.235 −17.152 1.00 48.82 O ATOM 5298 CB ARG C 147 22.378 37.515 −16.756 1.00 56.58 C ATOM 5299 CG ARG C 147 22.235 39.018 −16.790 1.00 68.10 C ATOM 5300 CD ARG C 147 21.709 39.524 −15.464 1.00 73.30 C ATOM 5301 NE ARG C 147 21.190 40.878 −15.583 1.00 85.24 N ATOM 5302 CZ ARG C 147 20.273 41.390 −14.773 1.00 88.04 C ATOM 5303 NH1 ARG C 147 19.780 40.651 −13.790 1.00 92.61 N ATOM 5304 NH2 ARG C 147 19.846 42.634 −14.949 1.00 84.03 N ATOM 5305 N ALA C 148 22.613 34.518 −17.996 1.00 48.93 N ATOM 5306 CA ALA C 148 22.941 33.124 −17.745 1.00 51.60 C ATOM 5307 C ALA C 148 24.169 32.739 −18.563 1.00 41.90 C ATOM 5308 O ALA C 148 24.961 31.883 −18.157 1.00 41.02 O ATOM 5309 CB ALA C 148 21.761 32.227 −18.076 1.00 35.92 C ATOM 5310 N ARG C 149 24.326 33.399 −19.705 1.00 32.02 N ATOM 5311 CA ARG C 149 25.438 33.115 −20.602 1.00 49.50 C ATOM 5312 C ARG C 149 26.758 33.772 −20.204 1.00 46.90 C ATOM 5313 O ARG C 149 27.829 33.172 −20.357 1.00 35.31 O ATOM 5314 CB ARG C 149 25.066 33.455 −22.042 1.00 47.87 C ATOM 5315 CG ARG C 149 24.204 32.383 −22.654 1.00 49.50 C ATOM 5316 CD ARG C 149 23.805 32.689 −24.070 1.00 52.59 C ATOM 5317 NE ARG C 149 22.734 31.784 −24.466 1.00 59.22 N ATOM 5318 CZ ARG C 149 21.836 32.053 −25.403 1.00 59.63 C ATOM 5319 NH1 ARG C 149 21.880 33.210 −26.053 1.00 57.37 N ATOM 5320 NH2 ARG C 149 20.893 31.166 −25.684 1.00 70.46 N ATOM 5321 N ALA C 150 26.682 34.996 −19.695 1.00 38.49 N ATOM 5322 CA ALA C 150 27.861 35.639 −19.146 1.00 38.00 C ATOM 5323 C ALA C 150 28.436 34.789 −18.006 1.00 37.45 C ATOM 5324 O ALA C 150 29.655 34.606 −17.906 1.00 34.48 O ATOM 5325 CB ALA C 150 27.531 37.043 −18.672 1.00 42.06 C ATOM 5326 N LYS C 151 27.563 34.259 −17.152 1.00 32.72 N ATOM 5327 CA LYS C 151 28.011 33.334 −16.117 1.00 34.60 C ATOM 5328 C LYS C 151 28.687 32.121 −16.759 1.00 40.36 C ATOM 5329 O LYS C 151 29.792 31.729 −16.364 1.00 37.01 O ATOM 5330 CB LYS C 151 26.859 32.882 −15.222 1.00 24.47 C ATOM 5331 CG LYS C 151 26.330 33.936 −14.273 1.00 41.34 C ATOM 5332 CD LYS C 151 25.225 33.335 −13.401 1.00 60.74 C ATOM 5333 CE LYS C 151 24.119 34.334 −13.075 1.00 64.62 C ATOM 5334 NZ LYS C 151 22.811 33.631 −12.871 1.00 66.54 N ATOM 5335 N VAL C 152 28.026 31.534 −17.755 1.00 38.63 N ATOM 5336 CA VAL C 152 28.615 30.414 −18.482 1.00 36.95 C ATOM 5337 C VAL C 152 29.957 30.818 −19.105 1.00 32.22 C ATOM 5338 O VAL C 152 30.914 30.056 −19.073 1.00 30.31 O ATOM 5339 CB VAL C 152 27.662 29.838 −19.545 1.00 35.07 C ATOM 5340 CG1 VAL C 152 28.418 28.960 −20.529 1.00 38.03 C ATOM 5341 CG2 VAL C 152 26.577 29.039 −18.876 1.00 34.35 C ATOM 5342 N ILE C 153 30.035 32.025 −19.646 1.00 28.98 N ATOM 5343 CA ILE C 153 31.304 32.517 −20.172 1.00 32.17 C ATOM 5344 C ILE C 153 32.361 32.665 −19.081 1.00 28.11 C ATOM 5345 O ILE C 153 33.489 32.203 −19.243 1.00 25.63 O ATOM 5346 CB ILE C 153 31.141 33.856 −20.902 1.00 28.28 C ATOM 5347 CG1 ILE C 153 30.243 33.675 −22.122 1.00 31.14 C ATOM 5348 CG2 ILE C 153 32.507 34.416 −21.307 1.00 25.39 C ATOM 5349 CD1 ILE C 153 29.962 34.942 −22.865 1.00 28.36 C ATOM 5350 N ILE C 154 32.002 33.316 −17.979 1.00 25.66 N ATOM 5351 CA ILE C 154 32.936 33.477 −16.864 1.00 32.11 C ATOM 5352 C ILE C 154 33.487 32.121 −16.402 1.00 32.41 C ATOM 5353 O ILE C 154 34.701 31.929 −16.270 1.00 24.04 O ATOM 5354 CB ILE C 154 32.286 34.211 −15.676 1.00 28.97 C ATOM 5355 CG1 ILE C 154 32.239 35.720 −15.952 1.00 35.49 C ATOM 5356 CG2 ILE C 154 33.060 33.930 −14.400 1.00 21.81 C ATOM 5357 CD1 ILE C 154 31.095 36.455 −15.254 1.00 29.02 C ATOM 5358 N CYS C 155 32.585 31.174 −16.176 1.00 28.52 N ATOM 5359 CA CYS C 155 32.987 29.827 −15.809 1.00 24.48 C ATOM 5360 C CYS C 155 33.971 29.196 −16.792 1.00 32.40 C ATOM 5361 O CYS C 155 34.907 28.508 −16.387 1.00 35.16 O ATOM 5362 CB CYS C 155 31.761 28.943 −15.659 1.00 19.97 C ATOM 5363 SG CYS C 155 30.897 29.287 −14.147 1.00 48.12 S ATOM 5364 N THR C 156 33.753 29.423 −18.083 1.00 28.13 N ATOM 5365 CA THR C 156 34.612 28.849 −19.104 1.00 29.38 C ATOM 5366 C THR C 156 36.013 29.479 −19.074 1.00 23.96 C ATOM 5367 O THR C 156 37.010 28.779 −19.189 1.00 21.72 O ATOM 5368 CB THR C 156 33.952 28.915 −20.498 1.00 22.69 C ATOM 5369 OG1 THR C 156 32.681 28.269 −20.426 1.00 37.62 O ATOM 5370 CG2 THR C 156 34.789 28.179 −21.531 1.00 19.20 C ATOM 5371 N VAL C 157 36.084 30.789 −18.881 1.00 21.52 N ATOM 5372 CA VAL C 157 37.373 31.434 −18.652 1.00 29.93 C ATOM 5373 C VAL C 157 38.132 30.841 −17.436 1.00 28.17 C ATOM 5374 O VAL C 157 39.334 30.589 −17.511 1.00 28.85 O ATOM 5375 CB VAL C 157 37.239 32.974 −18.540 1.00 22.91 C ATOM 5376 CG1 VAL C 157 38.554 33.617 −18.066 1.00 19.45 C ATOM 5377 CG2 VAL C 157 36.819 33.550 −19.870 1.00 20.63 C ATOM 5378 N TRP C 158 37.445 30.596 −16.328 1.00 19.54 N ATOM 5379 CA TRP C 158 38.135 30.015 −15.181 1.00 21.71 C ATOM 5380 C TRP C 158 38.560 28.564 −15.437 1.00 22.61 C ATOM 5381 O TRP C 158 39.521 28.094 −14.849 1.00 19.12 O ATOM 5382 CB TRP C 158 37.308 30.144 −13.888 1.00 25.05 C ATOM 5383 CG TRP C 158 37.359 31.528 −13.259 1.00 23.18 C ATOM 5384 CD1 TRP C 158 36.491 32.555 −13.478 1.00 21.39 C ATOM 5385 CD2 TRP C 158 38.337 32.027 −12.333 1.00 27.65 C ATOM 5386 NE1 TRP C 158 36.862 33.657 −12.754 1.00 23.44 N ATOM 5387 CE2 TRP C 158 37.989 33.364 −12.041 1.00 26.37 C ATOM 5388 CE3 TRP C 158 39.473 31.478 −11.728 1.00 28.95 C ATOM 5389 CZ2 TRP C 158 38.729 34.158 −11.168 1.00 25.78 C ATOM 5390 CZ3 TRP C 158 40.210 32.270 −10.861 1.00 32.81 C ATOM 5391 CH2 TRP C 158 39.836 33.596 −10.592 1.00 34.60 C ATOM 5392 N ALA C 159 37.854 27.856 −16.317 1.00 22.63 N ATOM 5393 CA ALA C 159 38.248 26.489 −16.660 1.00 22.27 C ATOM 5394 C ALA C 159 39.468 26.507 −17.575 1.00 22.85 C ATOM 5395 O ALA C 159 40.447 25.802 −17.344 1.00 20.45 O ATOM 5396 CB ALA C 159 37.101 25.737 −17.318 1.00 19.37 C ATOM 5397 N ILE C 160 39.389 27.318 −18.621 1.00 23.26 N ATOM 5398 CA ILE C 160 40.510 27.493 −19.527 1.00 26.52 C ATOM 5399 C ILE C 160 41.734 27.924 −18.731 1.00 30.29 C ATOM 5400 O ILE C 160 42.838 27.417 −18.948 1.00 28.49 O ATOM 5401 CB ILE C 160 40.195 28.510 −20.644 1.00 20.72 C ATOM 5402 CG1 ILE C 160 39.097 27.951 −21.555 1.00 26.76 C ATOM 5403 CG2 ILE C 160 41.442 28.821 −21.453 1.00 19.34 C ATOM 5404 CD1 ILE C 160 38.508 28.961 −22.549 1.00 23.67 C ATOM 5405 N SER C 161 41.530 28.845 −17.793 1.00 27.40 N ATOM 5406 CA SER C 161 42.635 29.336 −16.975 1.00 29.20 C ATOM 5407 C SER C 161 43.188 28.231 −16.098 1.00 21.40 C ATOM 5408 O SER C 161 44.390 28.088 −15.998 1.00 19.08 O ATOM 5409 CB SER C 161 42.229 30.548 −16.131 1.00 30.96 C ATOM 5410 OG SER C 161 42.010 31.691 −16.940 1.00 27.21 O ATOM 5411 N ALA C 162 42.308 27.446 −15.478 1.00 22.11 N ATOM 5412 CA ALA C 162 42.747 26.277 −14.717 1.00 25.25 C ATOM 5413 C ALA C 162 43.496 25.281 −15.611 1.00 28.31 C ATOM 5414 O ALA C 162 44.506 24.692 −15.208 1.00 22.76 O ATOM 5415 CB ALA C 162 41.571 25.594 −14.042 1.00 11.39 C ATOM 5416 N LEU C 163 42.999 25.099 −16.829 1.00 23.06 N ATOM 5417 CA LEU C 163 43.578 24.118 −17.723 1.00 24.50 C ATOM 5418 C LEU C 163 45.024 24.478 −18.074 1.00 26.00 C ATOM 5419 O LEU C 163 45.928 23.655 −17.924 1.00 21.79 O ATOM 5420 CB LEU C 163 42.728 23.963 −18.985 1.00 23.29 C ATOM 5421 CG LEU C 163 43.252 22.940 −19.997 1.00 27.50 C ATOM 5422 CD1 LEU C 163 43.251 21.534 −19.402 1.00 26.71 C ATOM 5423 CD2 LEU C 163 42.450 22.963 −21.271 1.00 25.71 C ATOM 5424 N VAL C 164 45.237 25.717 −18.505 1.00 28.36 N ATOM 5425 CA VAL C 164 46.531 26.143 −19.045 1.00 27.80 C ATOM 5426 C VAL C 164 47.580 26.587 −18.024 1.00 31.16 C ATOM 5427 O VAL C 164 48.742 26.782 −18.384 1.00 43.73 O ATOM 5428 CB VAL C 164 46.370 27.274 −20.084 1.00 25.39 C ATOM 5429 CG1 VAL C 164 45.413 26.844 −21.162 1.00 24.52 C ATOM 5430 CG2 VAL C 164 45.907 28.574 −19.418 1.00 20.12 C ATOM 5431 N SER C 165 47.192 26.746 −16.764 1.00 29.66 N ATOM 5432 CA SER C 165 48.142 27.244 −15.770 1.00 33.97 C ATOM 5433 C SER C 165 48.065 26.629 −14.371 1.00 30.41 C ATOM 5434 O SER C 165 49.031 26.688 −13.621 1.00 37.83 O ATOM 5435 CB SER C 165 48.114 28.782 −15.695 1.00 42.80 C ATOM 5436 OG SER C 165 46.820 29.311 −15.898 1.00 43.84 O ATOM 5437 N PHE C 166 46.936 26.043 −14.007 1.00 31.12 N ATOM 5438 CA PHE C 166 46.912 25.268 −12.773 1.00 31.81 C ATOM 5439 C PHE C 166 47.455 23.854 −13.010 1.00 28.48 C ATOM 5440 O PHE C 166 48.503 23.503 −12.489 1.00 31.99 O ATOM 5441 CB PHE C 166 45.509 25.216 −12.203 1.00 28.56 C ATOM 5442 CG PHE C 166 45.456 24.843 −10.761 1.00 25.44 C ATOM 5443 CD1 PHE C 166 45.254 23.531 −10.384 1.00 22.52 C ATOM 5444 CD2 PHE C 166 45.571 25.815 −9.775 1.00 32.27 C ATOM 5445 CE1 PHE C 166 45.184 23.186 −9.056 1.00 27.40 C ATOM 5446 CE2 PHE C 166 45.500 25.477 −8.432 1.00 28.83 C ATOM 5447 CZ PHE C 166 45.310 24.164 −8.072 1.00 33.51 C ATOM 5448 N LEU C 167 46.750 23.053 −13.801 1.00 25.12 N ATOM 5449 CA LEU C 167 47.198 21.689 −14.116 1.00 35.45 C ATOM 5450 C LEU C 167 48.704 21.480 −14.385 1.00 31.35 C ATOM 5451 O LEU C 167 49.310 20.617 −13.769 1.00 34.73 O ATOM 5452 CB LEU C 167 46.392 21.108 −15.284 1.00 35.20 C ATOM 5453 CG LEU C 167 44.961 20.687 −14.991 1.00 44.00 C ATOM 5454 CD1 LEU C 167 44.370 20.045 −16.238 1.00 47.63 C ATOM 5455 CD2 LEU C 167 44.940 19.722 −13.827 1.00 38.71 C ATOM 5456 N PRO C 168 49.301 22.243 −15.325 1.00 31.03 N ATOM 5457 CA PRO C 168 50.697 21.995 −15.702 1.00 29.22 C ATOM 5458 C PRO C 168 51.675 22.133 −14.543 1.00 27.03 C ATOM 5459 O PRO C 168 52.598 21.322 −14.426 1.00 29.00 O ATOM 5460 CB PRO C 168 50.972 23.078 −16.749 1.00 27.54 C ATOM 5461 CG PRO C 168 49.644 23.435 −17.285 1.00 22.08 C ATOM 5462 CD PRO C 168 48.720 23.339 −16.122 1.00 28.92 C ATOM 5463 N ILE C 169 51.482 23.154 −13.714 1.00 24.98 N ATOM 5464 CA ILE C 169 52.270 23.328 −12.494 1.00 28.25 C ATOM 5465 C ILE C 169 52.093 22.173 −11.510 1.00 27.60 C ATOM 5466 O ILE C 169 53.058 21.658 −10.954 1.00 33.49 O ATOM 5467 CB ILE C 169 51.934 24.656 −11.803 1.00 23.02 C ATOM 5468 CG1 ILE C 169 52.629 25.796 −12.550 1.00 24.11 C ATOM 5469 CG2 ILE C 169 52.371 24.626 −10.366 1.00 18.81 C ATOM 5470 CD1 ILE C 169 52.194 27.177 −12.178 1.00 16.50 C ATOM 5471 N MET C 170 50.850 21.762 −11.310 1.00 25.18 N ATOM 5472 CA MET C 170 50.555 20.588 −10.508 1.00 26.69 C ATOM 5473 C MET C 170 50.928 19.253 −11.180 1.00 36.71 C ATOM 5474 O MET C 170 50.998 18.230 −10.517 1.00 37.06 O ATOM 5475 CB MET C 170 49.082 20.600 −10.115 1.00 41.25 C ATOM 5476 CG MET C 170 48.666 21.838 −9.292 1.00 48.56 C ATOM 5477 SD MET C 170 48.966 21.710 −7.506 1.00 44.57 S ATOM 5478 CE MET C 170 50.739 21.941 −7.434 1.00 33.99 C ATOM 5479 N MET C 171 51.169 19.265 −12.487 1.00 37.67 N ATOM 5480 CA MET C 171 51.657 18.084 −13.191 1.00 39.60 C ATOM 5481 C MET C 171 53.193 18.051 −13.244 1.00 40.07 C ATOM 5482 O MET C 171 53.794 17.072 −13.701 1.00 32.95 O ATOM 5483 CB MET C 171 51.082 18.018 −14.611 1.00 41.02 C ATOM 5484 CG MET C 171 49.660 17.462 −14.718 1.00 38.96 C ATOM 5485 SD MET C 171 49.048 17.511 −16.430 1.00 52.12 S ATOM 5486 CE MET C 171 49.795 16.031 −17.113 1.00 40.51 C ATOM 5487 N HIS C 172 53.813 19.138 −12.793 1.00 38.07 N ATOM 5488 CA HIS C 172 55.268 19.218 −12.629 1.00 39.03 C ATOM 5489 C HIS C 172 56.038 19.449 −13.905 1.00 25.90 C ATOM 5490 O HIS C 172 57.226 19.169 −13.954 1.00 35.66 O ATOM 5491 CB HIS C 172 55.830 17.970 −11.939 1.00 40.31 C ATOM 5492 CG HIS C 172 55.121 17.615 −10.673 1.00 50.52 C ATOM 5493 ND1 HIS C 172 55.208 18.385 −9.534 1.00 50.52 N ATOM 5494 CD2 HIS C 172 54.303 16.578 −10.370 1.00 50.01 C ATOM 5495 CE1 HIS C 172 54.477 17.834 −8.579 1.00 54.33 C ATOM 5496 NE2 HIS C 172 53.917 16.739 −9.060 1.00 53.88 N ATOM 5497 N TRP C 173 55.378 19.964 −14.932 1.00 31.13 N ATOM 5498 CA TRP C 173 56.030 20.180 −16.223 1.00 29.61 C ATOM 5499 C TRP C 173 56.991 21.370 −16.184 1.00 35.21 C ATOM 5500 O TRP C 173 57.774 21.577 −17.110 1.00 34.17 O ATOM 5501 CB TRP C 173 54.977 20.434 −17.292 1.00 31.54 C ATOM 5502 CG TRP C 173 54.112 19.255 −17.634 1.00 31.81 C ATOM 5503 CD1 TRP C 173 54.102 18.025 −17.036 1.00 32.87 C ATOM 5504 CD2 TRP C 173 53.096 19.221 −18.639 1.00 27.89 C ATOM 5505 NE1 TRP C 173 53.146 17.224 −17.620 1.00 30.70 N ATOM 5506 CE2 TRP C 173 52.519 17.937 −18.609 1.00 34.12 C ATOM 5507 CE3 TRP C 173 52.615 20.158 −19.563 1.00 26.18 C ATOM 5508 CZ2 TRP C 173 51.490 17.566 −19.475 1.00 36.45 C ATOM 5509 CZ3 TRP C 173 51.594 19.793 −20.414 1.00 22.86 C ATOM 5510 CH2 TRP C 173 51.049 18.505 −20.372 1.00 28.04 C ATOM 5511 N TRP C 174 56.913 22.154 −15.114 1.00 28.74 N ATOM 5512 CA TRP C 174 57.661 23.392 −15.010 1.00 25.36 C ATOM 5513 C TRP C 174 59.093 23.147 −14.535 1.00 29.77 C ATOM 5514 O TRP C 174 59.911 24.070 −14.523 1.00 28.37 O ATOM 5515 CB TRP C 174 56.944 24.353 −14.047 1.00 31.67 C ATOM 5516 CG TRP C 174 56.792 23.783 −12.648 1.00 32.26 C ATOM 5517 CD1 TRP C 174 55.859 22.879 −12.233 1.00 30.07 C ATOM 5518 CD2 TRP C 174 57.609 24.067 −11.502 1.00 28.60 C ATOM 5519 NE1 TRP C 174 56.039 22.583 −10.904 1.00 33.83 N ATOM 5520 CE2 TRP C 174 57.108 23.295 −10.430 1.00 36.77 C ATOM 5521 CE3 TRP C 174 58.710 24.898 −11.276 1.00 31.63 C ATOM 5522 CZ2 TRP C 174 57.671 23.332 −9.148 1.00 32.27 C ATOM 5523 CZ3 TRP C 174 59.264 24.934 −10.000 1.00 36.95 C ATOM 5524 CH2 TRP C 174 58.742 24.156 −8.956 1.00 28.36 C ATOM 5525 N ARG C 175 59.404 21.912 −14.147 1.00 24.43 N ATOM 5526 CA ARG C 175 60.688 21.658 −13.482 1.00 35.43 C ATOM 5527 C ARG C 175 61.900 21.544 −14.408 1.00 32.95 C ATOM 5528 O ARG C 175 61.814 21.012 −15.515 1.00 29.79 O ATOM 5529 CB ARG C 175 60.622 20.453 −12.527 1.00 27.23 C ATOM 5530 CG ARG C 175 59.531 20.569 −11.481 1.00 33.16 C ATOM 5531 CD ARG C 175 59.972 20.026 −10.142 1.00 32.01 C ATOM 5532 NE ARG C 175 59.074 18.987 −9.651 1.00 47.03 N ATOM 5533 CZ ARG C 175 58.687 18.864 −8.384 1.00 62.54 C ATOM 5534 NH1 ARG C 175 59.100 19.736 −7.475 1.00 59.81 N ATOM 5535 NH2 ARG C 175 57.867 17.881 −8.030 1.00 66.33 N ATOM 5536 N ASP C 176 63.026 22.052 −13.916 1.00 30.02 N ATOM 5537 CA ASP C 176 64.297 22.000 −14.612 1.00 29.44 C ATOM 5538 C ASP C 176 65.041 20.741 −14.213 1.00 29.44 C ATOM 5539 O ASP C 176 64.587 19.997 −13.352 1.00 32.19 O ATOM 5540 CB ASP C 176 65.127 23.229 −14.269 1.00 40.94 C ATOM 5541 CG ASP C 176 66.082 23.614 −15.375 1.00 52.10 C ATOM 5542 OD1 ASP C 176 66.438 22.730 −16.181 1.00 50.29 O ATOM 5543 OD2 ASP C 176 66.468 24.804 −15.440 1.00 61.42 O ATOM 5544 N GLU C 177 66.183 20.502 −14.849 1.00 39.94 N ATOM 5545 CA GLU C 177 66.919 19.253 −14.671 1.00 46.66 C ATOM 5546 C GLU C 177 68.215 19.520 −13.914 1.00 50.47 C ATOM 5547 O GLU C 177 68.776 18.636 −13.251 1.00 32.00 O ATOM 5548 CB GLU C 177 67.207 18.621 −16.033 1.00 64.62 C ATOM 5549 CG GLU C 177 67.285 17.116 −15.974 1.00 89.42 C ATOM 5550 CD GLU C 177 66.411 16.553 −14.869 1.00 87.28 C ATOM 5551 OE1 GLU C 177 65.218 16.925 −14.812 1.00 85.94 O ATOM 5552 OE2 GLU C 177 66.916 15.747 −14.054 1.00 87.29 O ATOM 5553 N ASP C 178 68.646 20.775 −14.027 1.00 47.96 N ATOM 5554 CA ASP C 178 69.811 21.346 −13.358 1.00 44.10 C ATOM 5555 C ASP C 178 69.959 20.975 −11.889 1.00 45.88 C ATOM 5556 O ASP C 178 68.976 20.928 −11.151 1.00 53.65 O ATOM 5557 CB ASP C 178 69.726 22.871 −13.465 1.00 45.89 C ATOM 5558 CG ASP C 178 71.016 23.560 −13.069 1.00 64.23 C ATOM 5559 OD1 ASP C 178 72.099 23.017 −13.372 1.00 71.36 O ATOM 5560 OD2 ASP C 178 70.951 24.653 −12.467 1.00 68.05 O ATOM 5561 N PRO C 179 71.205 20.725 −11.457 1.00 54.24 N ATOM 5562 CA PRO C 179 71.586 20.584 −10.047 1.00 51.33 C ATOM 5563 C PRO C 179 70.915 21.612 −9.127 1.00 45.07 C ATOM 5564 O PRO C 179 70.292 21.232 −8.129 1.00 32.53 O ATOM 5565 CB PRO C 179 73.095 20.834 −10.087 1.00 46.19 C ATOM 5566 CG PRO C 179 73.513 20.302 −11.401 1.00 44.51 C ATOM 5567 CD PRO C 179 72.347 20.467 −12.353 1.00 46.52 C ATOM 5568 N GLN C 180 71.057 22.895 −9.451 1.00 36.91 N ATOM 5569 CA GLN C 180 70.498 23.952 −8.618 1.00 43.09 C ATOM 5570 C GLN C 180 68.982 23.841 −8.478 1.00 42.59 C ATOM 5571 O GLN C 180 68.433 24.029 −7.392 1.00 38.62 O ATOM 5572 CB GLN C 180 70.882 25.328 −9.153 1.00 51.52 C ATOM 5573 CG GLN C 180 72.325 25.702 −8.874 1.00 76.01 C ATOM 5574 CD GLN C 180 72.645 27.133 −9.259 1.00 108.26 C ATOM 5575 OE1 GLN C 180 71.749 27.975 −9.377 1.00 114.08 O ATOM 5576 NE2 GLN C 180 73.929 27.419 −9.455 1.00 116.20 N ATOM 5577 N ALA C 181 68.310 23.532 −9.579 1.00 36.06 N ATOM 5578 CA ALA C 181 66.874 23.326 −9.551 1.00 33.52 C ATOM 5579 C ALA C 181 66.538 22.182 −8.600 1.00 37.08 C ATOM 5580 O ALA C 181 65.696 22.331 −7.714 1.00 31.17 O ATOM 5581 CB ALA C 181 66.348 23.040 −10.946 1.00 34.36 C ATOM 5582 N LEU C 182 67.206 21.044 −8.775 1.00 36.19 N ATOM 5583 CA LEU C 182 66.949 19.881 −7.924 1.00 44.01 C ATOM 5584 C LEU C 182 67.191 20.189 −6.445 1.00 38.45 C ATOM 5585 O LEU C 182 66.449 19.730 −5.578 1.00 37.66 O ATOM 5586 CB LEU C 182 67.781 18.679 −8.369 1.00 47.13 C ATOM 5587 CG LEU C 182 67.336 18.039 −9.682 1.00 55.72 C ATOM 5588 CD1 LEU C 182 68.080 16.734 −9.909 1.00 58.51 C ATOM 5589 CD2 LEU C 182 65.827 17.810 −9.668 1.00 40.22 C ATOM 5590 N LYS C 183 68.235 20.967 −6.171 1.00 36.84 N ATOM 5591 CA LYS C 183 68.513 21.440 −4.820 1.00 38.02 C ATOM 5592 C LYS C 183 67.312 22.165 −4.245 1.00 37.82 C ATOM 5593 O LYS C 183 66.953 21.958 −3.090 1.00 32.61 O ATOM 5594 CB LYS C 183 69.701 22.389 −4.830 1.00 38.85 C ATOM 5595 CG LYS C 183 70.248 22.682 −3.467 1.00 42.96 C ATOM 5596 CD LYS C 183 71.615 23.334 −3.559 1.00 48.91 C ATOM 5597 CE LYS C 183 72.159 23.638 −2.173 1.00 61.15 C ATOM 5598 NZ LYS C 183 73.271 24.623 −2.229 1.00 79.11 N ATOM 5599 N CYS C 184 66.693 23.013 −5.063 1.00 36.90 N ATOM 5600 CA CYS C 184 65.548 23.798 −4.625 1.00 35.14 C ATOM 5601 C CYS C 184 64.328 22.922 −4.343 1.00 38.13 C ATOM 5602 O CYS C 184 63.638 23.095 −3.325 1.00 37.28 O ATOM 5603 CB CYS C 184 65.197 24.867 −5.660 1.00 33.65 C ATOM 5604 SG CYS C 184 63.834 25.960 −5.135 1.00 67.53 S ATOM 5605 N TYR C 185 64.064 21.980 −5.242 1.00 30.92 N ATOM 5606 CA TYR C 185 62.882 21.143 −5.119 1.00 32.04 C ATOM 5607 C TYR C 185 62.885 20.307 −3.844 1.00 33.53 C ATOM 5608 O TYR C 185 61.839 19.843 −3.391 1.00 35.47 O ATOM 5609 CB TYR C 185 62.711 20.245 −6.342 1.00 38.39 C ATOM 5610 CG TYR C 185 62.687 20.998 −7.645 1.00 35.05 C ATOM 5611 CD1 TYR C 185 62.214 22.303 −7.701 1.00 23.91 C ATOM 5612 CD2 TYR C 185 63.142 20.401 −8.825 1.00 28.95 C ATOM 5613 CE1 TYR C 185 62.202 23.003 −8.903 1.00 35.32 C ATOM 5614 CE2 TYR C 185 63.136 21.088 −10.032 1.00 26.73 C ATOM 5615 CZ TYR C 185 62.659 22.387 −10.067 1.00 31.32 C ATOM 5616 OH TYR C 185 62.633 23.083 −11.254 1.00 27.71 O ATOM 5617 N GLN C 186 64.055 20.134 −3.246 1.00 36.31 N ATOM 5618 CA GLN C 186 64.146 19.314 −2.046 1.00 45.11 C ATOM 5619 C GLN C 186 64.266 20.113 −0.756 1.00 37.94 C ATOM 5620 O GLN C 186 64.208 19.556 0.340 1.00 42.51 O ATOM 5621 CB GLN C 186 65.276 18.305 −2.168 1.00 45.70 C ATOM 5622 CG GLN C 186 64.867 17.079 −2.938 1.00 45.66 C ATOM 5623 CD GLN C 186 65.593 15.875 −2.455 1.00 70.76 C ATOM 5624 OE1 GLN C 186 66.211 15.903 −1.388 1.00 91.13 O ATOM 5625 NE2 GLN C 186 65.539 14.801 −3.230 1.00 92.01 N ATOM 5626 N ASP C 187 64.433 21.418 −0.893 1.00 28.09 N ATOM 5627 CA ASP C 187 64.446 22.285 0.263 1.00 37.87 C ATOM 5628 C ASP C 187 63.039 22.845 0.455 1.00 33.83 C ATOM 5629 O ASP C 187 62.585 23.644 −0.372 1.00 35.60 O ATOM 5630 CB ASP C 187 65.463 23.410 0.059 1.00 35.90 C ATOM 5631 CG ASP C 187 65.545 24.366 1.255 1.00 49.41 C ATOM 5632 OD1 ASP C 187 65.042 24.033 2.358 1.00 40.36 O ATOM 5633 OD2 ASP C 187 66.122 25.465 1.081 1.00 60.45 O ATOM 5634 N PRO C 188 62.337 22.404 1.527 1.00 23.88 N ATOM 5635 CA PRO C 188 60.997 22.904 1.847 1.00 26.25 C ATOM 5636 C PRO C 188 61.015 24.402 2.097 1.00 29.14 C ATOM 5637 O PRO C 188 59.987 25.076 2.004 1.00 32.09 O ATOM 5638 CB PRO C 188 60.628 22.144 3.117 1.00 17.62 C ATOM 5639 CG PRO C 188 61.377 20.897 3.033 1.00 20.77 C ATOM 5640 CD PRO C 188 62.684 21.245 2.361 1.00 29.00 C ATOM 5641 N GLY C 189 62.195 24.923 2.387 1.00 28.73 N ATOM 5642 CA GLY C 189 62.357 26.350 2.559 1.00 30.99 C ATOM 5643 C GLY C 189 62.444 27.109 1.252 1.00 25.17 C ATOM 5644 O GLY C 189 62.091 28.285 1.191 1.00 33.60 O ATOM 5645 N CYS C 190 62.925 26.457 0.203 1.00 26.66 N ATOM 5646 CA CYS C 190 63.029 27.134 −1.090 1.00 42.07 C ATOM 5647 C CYS C 190 61.710 27.073 −1.879 1.00 39.35 C ATOM 5648 O CYS C 190 61.181 25.983 −2.144 1.00 38.96 O ATOM 5649 CB CYS C 190 64.199 26.584 −1.914 1.00 31.69 C ATOM 5650 SG CYS C 190 64.300 27.254 −3.599 1.00 51.78 S ATOM 5651 N CYS C 191 61.179 28.249 −2.215 1.00 31.71 N ATOM 5652 CA CYS C 191 59.986 28.359 −3.058 1.00 37.21 C ATOM 5653 C CYS C 191 60.253 29.243 −4.276 1.00 40.09 C ATOM 5654 O CYS C 191 59.476 30.148 −4.575 1.00 45.07 O ATOM 5655 CB CYS C 191 58.775 28.896 −2.269 1.00 28.12 C ATOM 5656 SG CYS C 191 57.129 28.402 −2.949 1.00 30.69 S ATOM 5657 N ASP C 192 61.360 28.988 −4.967 1.00 47.32 N ATOM 5658 CA ASP C 192 61.677 29.701 −6.200 1.00 36.52 C ATOM 5659 C ASP C 192 60.978 29.019 −7.336 1.00 37.88 C ATOM 5660 O ASP C 192 61.017 27.791 −7.456 1.00 44.51 O ATOM 5661 CB ASP C 192 63.169 29.662 −6.500 1.00 37.78 C ATOM 5662 CG ASP C 192 63.985 30.443 −5.512 1.00 56.08 C ATOM 5663 OD1 ASP C 192 63.523 30.621 −4.365 1.00 66.20 O ATOM 5664 OD2 ASP C 192 65.097 30.871 −5.887 1.00 73.78 O ATOM 5665 N PHE C 193 60.345 29.809 −8.186 1.00 38.40 N ATOM 5666 CA PHE C 193 59.734 29.242 −9.377 1.00 42.86 C ATOM 5667 C PHE C 193 60.826 29.061 −10.442 1.00 37.32 C ATOM 5668 O PHE C 193 60.876 29.776 −11.453 1.00 38.86 O ATOM 5669 CB PHE C 193 58.562 30.106 −9.858 1.00 30.64 C ATOM 5670 CG PHE C 193 57.594 29.376 −10.722 1.00 31.35 C ATOM 5671 CD1 PHE C 193 57.341 28.024 −10.505 1.00 27.69 C ATOM 5672 CD2 PHE C 193 56.920 30.036 −11.744 1.00 25.39 C ATOM 5673 CE1 PHE C 193 56.433 27.337 −11.298 1.00 23.99 C ATOM 5674 CE2 PHE C 193 56.021 29.366 −12.538 1.00 25.98 C ATOM 5675 CZ PHE C 193 55.775 28.005 −12.312 1.00 26.70 C ATOM 5676 N VAL C 194 61.712 28.107 −10.168 1.00 30.15 N ATOM 5677 CA VAL C 194 62.812 27.748 −11.053 1.00 31.15 C ATOM 5678 C VAL C 194 62.300 26.786 −12.116 1.00 31.06 C ATOM 5679 O VAL C 194 62.051 25.608 −11.831 1.00 29.20 O ATOM 5680 CB VAL C 194 63.937 27.059 −10.254 1.00 30.98 C ATOM 5681 CG1 VAL C 194 65.036 26.558 −11.182 1.00 29.95 C ATOM 5682 CG2 VAL C 194 64.481 27.995 −9.218 1.00 21.89 C ATOM 5683 N THR C 195 62.143 27.277 −13.341 1.00 28.88 N ATOM 5684 CA THR C 195 61.483 26.479 −14.374 1.00 31.24 C ATOM 5685 C THR C 195 62.402 26.162 −15.533 1.00 29.23 C ATOM 5686 O THR C 195 63.382 26.863 −15.763 1.00 41.30 O ATOM 5687 CB THR C 195 60.205 27.172 −14.899 1.00 32.41 C ATOM 5688 OG1 THR C 195 60.541 28.442 −15.472 1.00 31.47 O ATOM 5689 CG2 THR C 195 59.218 27.403 −13.759 1.00 35.99 C ATOM 5690 N ASN C 196 62.090 25.096 −16.258 1.00 30.93 N ATOM 5691 CA ASN C 196 62.798 24.824 −17.499 1.00 33.28 C ATOM 5692 C ASN C 196 62.417 25.866 −18.552 1.00 26.49 C ATOM 5693 O ASN C 196 61.333 26.455 −18.490 1.00 25.97 O ATOM 5694 CB ASN C 196 62.548 23.390 −17.976 1.00 30.77 C ATOM 5695 CG ASN C 196 61.118 23.152 −18.401 1.00 27.68 C ATOM 5696 OD1 ASN C 196 60.604 23.810 −19.298 1.00 30.67 O ATOM 5697 ND2 ASN C 196 60.478 22.185 −17.778 1.00 25.76 N ATOM 5698 N ARG C 197 63.311 26.111 −19.503 1.00 33.24 N ATOM 5699 CA ARG C 197 63.108 27.204 −20.464 1.00 37.94 C ATOM 5700 C ARG C 197 61.921 26.994 −21.415 1.00 28.30 C ATOM 5701 O ARG C 197 61.290 27.958 −21.859 1.00 27.80 O ATOM 5702 CB ARG C 197 64.393 27.499 −21.244 1.00 31.42 C ATOM 5703 CG ARG C 197 65.524 28.031 −20.372 1.00 46.04 C ATOM 5704 CD ARG C 197 66.675 28.573 −21.193 1.00 44.31 C ATOM 5705 NE ARG C 197 67.804 28.957 −20.351 1.00 63.52 N ATOM 5706 CZ ARG C 197 68.931 29.494 −20.809 1.00 88.38 C ATOM 5707 NH1 ARG C 197 69.092 29.716 −22.112 1.00 98.54 N ATOM 5708 NH2 ARG C 197 69.900 29.813 −19.964 1.00 86.98 N ATOM 5709 N ALA C 198 61.617 25.740 −21.724 1.00 19.46 N ATOM 5710 CA ALA C 198 60.474 25.448 −22.566 1.00 15.92 C ATOM 5711 C ALA C 198 59.233 25.994 −21.879 1.00 29.45 C ATOM 5712 O ALA C 198 58.508 26.814 −22.443 1.00 30.53 O ATOM 5713 CB ALA C 198 60.346 23.961 −22.796 1.00 21.39 C ATOM 5714 N TYR C 199 59.013 25.562 −20.640 1.00 31.13 N ATOM 5715 CA TYR C 199 57.833 25.957 −19.890 1.00 21.47 C ATOM 5716 C TYR C 199 57.782 27.463 −19.642 1.00 24.81 C ATOM 5717 O TYR C 199 56.707 28.055 −19.636 1.00 26.38 O ATOM 5718 CB TYR C 199 57.734 25.182 −18.575 1.00 24.21 C ATOM 5719 CG TYR C 199 56.668 25.735 −17.674 1.00 26.87 C ATOM 5720 CD1 TYR C 199 55.439 25.103 −17.540 1.00 30.48 C ATOM 5721 CD2 TYR C 199 56.877 26.920 −16.981 1.00 25.91 C ATOM 5722 CE1 TYR C 199 54.453 25.634 −16.717 1.00 27.59 C ATOM 5723 CE2 TYR C 199 55.913 27.454 −16.175 1.00 28.37 C ATOM 5724 CZ TYR C 199 54.707 26.812 −16.038 1.00 28.45 C ATOM 5725 OH TYR C 199 53.764 27.378 −15.215 1.00 35.19 O ATOM 5726 N ALA C 200 58.936 28.091 −19.442 1.00 31.16 N ATOM 5727 CA ALA C 200 58.965 29.543 −19.252 1.00 34.83 C ATOM 5728 C ALA C 200 58.360 30.277 −20.452 1.00 32.63 C ATOM 5729 O ALA C 200 57.545 31.185 −20.297 1.00 30.06 O ATOM 5730 CB ALA C 200 60.367 30.026 −18.994 1.00 23.20 C ATOM 5731 N ILE C 201 58.753 29.879 −21.653 1.00 28.67 N ATOM 5732 CA ILE C 201 58.248 30.536 −22.853 1.00 33.86 C ATOM 5733 C ILE C 201 56.796 30.161 −23.182 1.00 29.79 C ATOM 5734 O ILE C 201 55.940 31.028 −23.350 1.00 26.16 O ATOM 5735 CB ILE C 201 59.157 30.245 −24.054 1.00 32.01 C ATOM 5736 CG1 ILE C 201 60.477 31.014 −23.909 1.00 34.90 C ATOM 5737 CG2 ILE C 201 58.457 30.640 −25.335 1.00 27.43 C ATOM 5738 CD1 ILE C 201 61.650 30.355 −24.604 1.00 22.93 C ATOM 5739 N ALA C 202 56.519 28.868 −23.260 1.00 22.73 N ATOM 5740 CA ALA C 202 55.185 28.415 −23.592 1.00 21.85 C ATOM 5741 C ALA C 202 54.145 29.114 −22.734 1.00 29.37 C ATOM 5742 O ALA C 202 53.169 29.661 −23.250 1.00 29.11 O ATOM 5743 CB ALA C 202 55.079 26.901 −23.445 1.00 19.66 C ATOM 5744 N SER C 203 54.373 29.111 −21.423 1.00 30.30 N ATOM 5745 CA SER C 203 53.371 29.580 −20.461 1.00 29.60 C ATOM 5746 C SER C 203 53.211 31.102 −20.358 1.00 27.17 C ATOM 5747 O SER C 203 52.124 31.573 −20.044 1.00 23.95 O ATOM 5748 CB SER C 203 53.614 28.978 −19.078 1.00 24.83 C ATOM 5749 OG SER C 203 54.656 29.657 −18.419 1.00 34.61 O ATOM 5750 N SER C 204 54.262 31.881 −20.609 1.00 24.73 N ATOM 5751 CA SER C 204 54.048 33.328 −20.637 1.00 33.01 C ATOM 5752 C SER C 204 53.302 33.748 −21.905 1.00 32.93 C ATOM 5753 O SER C 204 52.386 34.578 −21.850 1.00 31.00 O ATOM 5754 CB SER C 204 55.322 34.160 −20.387 1.00 24.42 C ATOM 5755 OG SER C 204 56.488 33.383 −20.490 1.00 35.81 O ATOM 5756 N ILE C 205 53.665 33.149 −23.033 1.00 24.78 N ATOM 5757 CA ILE C 205 52.935 33.386 −24.268 1.00 27.32 C ATOM 5758 C ILE C 205 51.458 33.019 −24.134 1.00 30.61 C ATOM 5759 O ILE C 205 50.577 33.789 −24.498 1.00 34.02 O ATOM 5760 CB ILE C 205 53.510 32.564 −25.406 1.00 24.47 C ATOM 5761 CG1 ILE C 205 54.884 33.113 −25.798 1.00 28.65 C ATOM 5762 CG2 ILE C 205 52.547 32.558 −26.585 1.00 19.52 C ATOM 5763 CD1 ILE C 205 55.715 32.133 −26.627 1.00 24.39 C ATOM 5764 N ILE C 206 51.202 31.837 −23.592 1.00 29.27 N ATOM 5765 CA ILE C 206 49.861 31.271 −23.524 1.00 22.78 C ATOM 5766 C ILE C 206 48.993 31.878 −22.435 1.00 27.48 C ATOM 5767 O ILE C 206 47.792 32.012 −22.607 1.00 32.04 O ATOM 5768 CB ILE C 206 49.937 29.754 −23.290 1.00 22.98 C ATOM 5769 CG1 ILE C 206 50.369 29.051 −24.569 1.00 27.24 C ATOM 5770 CG2 ILE C 206 48.614 29.214 −22.802 1.00 24.96 C ATOM 5771 CD1 ILE C 206 50.541 27.578 −24.405 1.00 37.77 C ATOM 5772 N SER C 207 49.600 32.236 −21.306 1.00 37.22 N ATOM 5773 CA SER C 207 48.848 32.766 −20.166 1.00 30.09 C ATOM 5774 C SER C 207 48.748 34.292 −20.208 1.00 36.11 C ATOM 5775 O SER C 207 47.855 34.876 −19.589 1.00 34.82 O ATOM 5776 CB SER C 207 49.470 32.315 −18.838 1.00 24.50 C ATOM 5777 OG SER C 207 49.502 30.901 −18.708 1.00 27.16 O ATOM 5778 N PHE C 208 49.658 34.933 −20.944 1.00 30.50 N ATOM 5779 CA PHE C 208 49.737 36.392 −20.946 1.00 29.29 C ATOM 5780 C PHE C 208 49.828 37.028 −22.359 1.00 33.44 C ATOM 5781 O PHE C 208 48.979 37.836 −22.730 1.00 33.61 O ATOM 5782 CB PHE C 208 50.889 36.845 −20.037 1.00 26.34 C ATOM 5783 CG PHE C 208 50.984 38.332 −19.859 1.00 31.24 C ATOM 5784 CD1 PHE C 208 50.208 38.984 −18.914 1.00 28.16 C ATOM 5785 CD2 PHE C 208 51.870 39.084 −20.628 1.00 35.39 C ATOM 5786 CE1 PHE C 208 50.308 40.358 −18.741 1.00 28.80 C ATOM 5787 CE2 PHE C 208 51.968 40.466 −20.466 1.00 32.25 C ATOM 5788 CZ PHE C 208 51.189 41.099 −19.527 1.00 31.77 C ATOM 5789 N TYR C 209 50.833 36.669 −23.152 1.00 32.43 N ATOM 5790 CA TYR C 209 51.063 37.371 −24.425 1.00 35.84 C ATOM 5791 C TYR C 209 49.910 37.339 −25.410 1.00 35.04 C ATOM 5792 O TYR C 209 49.412 38.387 −25.820 1.00 39.66 O ATOM 5793 CB TYR C 209 52.379 36.943 −25.087 1.00 29.59 C ATOM 5794 CG TYR C 209 53.529 37.549 −24.343 1.00 41.44 C ATOM 5795 CD1 TYR C 209 54.305 36.785 −23.478 1.00 38.26 C ATOM 5796 CD2 TYR C 209 53.781 38.911 −24.428 1.00 36.52 C ATOM 5797 CE1 TYR C 209 55.334 37.355 −22.751 1.00 31.75 C ATOM 5798 CE2 TYR C 209 54.805 39.490 −23.707 1.00 43.61 C ATOM 5799 CZ TYR C 209 55.577 38.709 −22.870 1.00 38.87 C ATOM 5800 OH TYR C 209 56.595 39.298 −22.164 1.00 34.79 O ATOM 5801 N ILE C 210 49.493 36.142 −25.795 1.00 32.37 N ATOM 5802 CA ILE C 210 48.319 35.978 −26.645 1.00 30.16 C ATOM 5803 C ILE C 210 47.089 36.740 −26.143 1.00 36.22 C ATOM 5804 O ILE C 210 46.544 37.582 −26.866 1.00 37.50 O ATOM 5805 CB ILE C 210 47.959 34.508 −26.794 1.00 26.00 C ATOM 5806 CG1 ILE C 210 48.964 33.828 −27.719 1.00 26.31 C ATOM 5807 CG2 ILE C 210 46.539 34.364 −27.311 1.00 32.16 C ATOM 5808 CD1 ILE C 210 48.899 32.327 −27.661 1.00 31.77 C ATOM 5809 N PRO C 211 46.642 36.450 −24.904 1.00 34.80 N ATOM 5810 CA PRO C 211 45.468 37.173 −24.404 1.00 32.95 C ATOM 5811 C PRO C 211 45.708 38.677 −24.386 1.00 34.21 C ATOM 5812 O PRO C 211 44.754 39.454 −24.468 1.00 34.81 O ATOM 5813 CB PRO C 211 45.308 36.650 −22.972 1.00 23.44 C ATOM 5814 CG PRO C 211 46.024 35.339 −22.966 1.00 30.36 C ATOM 5815 CD PRO C 211 47.160 35.487 −23.915 1.00 31.02 C ATOM 5816 N LEU C 212 46.968 39.086 −24.281 1.00 28.26 N ATOM 5817 CA LEU C 212 47.262 40.504 −24.178 1.00 33.81 C ATOM 5818 C LEU C 212 47.147 41.166 −25.537 1.00 41.29 C ATOM 5819 O LEU C 212 46.492 42.193 −25.693 1.00 41.28 O ATOM 5820 CB LEU C 212 48.653 40.742 −23.625 1.00 31.92 C ATOM 5821 CG LEU C 212 48.850 42.253 −23.566 1.00 33.51 C ATOM 5822 CD1 LEU C 212 48.232 42.764 −22.293 1.00 33.76 C ATOM 5823 CD2 LEU C 212 50.322 42.622 −23.666 1.00 35.51 C ATOM 5824 N LEU C 213 47.809 40.575 −26.519 1.00 34.93 N ATOM 5825 CA LEU C 213 47.684 41.042 −27.878 1.00 34.75 C ATOM 5826 C LEU C 213 46.208 41.169 −28.246 1.00 38.02 C ATOM 5827 O LEU C 213 45.738 42.270 −28.518 1.00 38.36 O ATOM 5828 CB LEU C 213 48.433 40.109 −28.821 1.00 36.33 C ATOM 5829 CG LEU C 213 49.895 40.063 −28.373 1.00 45.19 C ATOM 5830 CD1 LEU C 213 50.750 39.140 −29.241 1.00 38.50 C ATOM 5831 CD2 LEU C 213 50.470 41.477 −28.341 1.00 36.87 C ATOM 5832 N ILE C 214 45.473 40.058 −28.215 1.00 34.84 N ATOM 5833 CA ILE C 214 44.048 40.090 −28.534 1.00 36.72 C ATOM 5834 C ILE C 214 43.351 41.260 −27.842 1.00 41.26 C ATOM 5835 O ILE C 214 42.662 42.050 −28.482 1.00 42.24 O ATOM 5836 CB ILE C 214 43.331 38.786 −28.146 1.00 30.17 C ATOM 5837 CG1 ILE C 214 43.700 37.673 −29.107 1.00 25.82 C ATOM 5838 CG2 ILE C 214 41.823 38.963 −28.188 1.00 24.22 C ATOM 5839 CD1 ILE C 214 43.312 36.302 −28.589 1.00 27.14 C ATOM 5840 N MET C 215 43.533 41.382 −26.535 1.00 35.35 N ATOM 5841 CA MET C 215 42.855 42.445 −25.817 1.00 38.41 C ATOM 5842 C MET C 215 43.260 43.818 −26.310 1.00 40.10 C ATOM 5843 O MET C 215 42.438 44.716 −26.379 1.00 41.92 O ATOM 5844 CB MET C 215 43.122 42.376 −24.325 1.00 46.52 C ATOM 5845 CG MET C 215 42.452 43.525 −23.587 1.00 53.39 C ATOM 5846 SD MET C 215 43.138 43.840 −21.962 1.00 55.64 S ATOM 5847 CE MET C 215 44.790 44.371 −22.399 1.00 37.25 C ATOM 5848 N ILE C 216 44.534 43.985 −26.633 1.00 48.12 N ATOM 5849 CA ILE C 216 45.043 45.263 −27.067 1.00 47.21 C ATOM 5850 C ILE C 216 44.409 45.683 −28.397 1.00 47.60 C ATOM 5851 O ILE C 216 43.878 46.788 −28.534 1.00 45.96 O ATOM 5852 CB ILE C 216 46.598 45.283 −27.153 1.00 52.91 C ATOM 5853 CG1 ILE C 216 47.201 45.641 −25.788 1.00 51.26 C ATOM 5854 CG2 ILE C 216 47.093 46.250 −28.222 1.00 44.85 C ATOM 5855 CD1 ILE C 216 48.677 45.304 −25.648 1.00 39.51 C ATOM 5856 N PHE C 217 44.460 44.763 −29.357 1.00 46.49 N ATOM 5857 CA PHE C 217 43.843 44.922 −30.670 1.00 46.01 C ATOM 5858 C PHE C 217 42.351 45.248 −30.541 1.00 50.54 C ATOM 5859 O PHE C 217 41.921 46.374 −30.797 1.00 52.61 O ATOM 5860 CB PHE C 217 44.061 43.626 −31.471 1.00 47.24 C ATOM 5861 CG PHE C 217 43.406 43.602 −32.836 1.00 71.74 C ATOM 5862 CD1 PHE C 217 44.154 43.838 −33.986 1.00 74.87 C ATOM 5863 CD2 PHE C 217 42.054 43.297 −32.976 1.00 66.24 C ATOM 5864 CE1 PHE C 217 43.560 43.796 −35.248 1.00 72.23 C ATOM 5865 CE2 PHE C 217 41.455 43.256 −34.235 1.00 62.21 C ATOM 5866 CZ PHE C 217 42.211 43.505 −35.370 1.00 62.00 C ATOM 5867 N VAL C 218 41.570 44.257 −30.126 1.00 45.10 N ATOM 5868 CA VAL C 218 40.133 44.402 −30.017 1.00 34.84 C ATOM 5869 C VAL C 218 39.805 45.717 −29.323 1.00 39.29 C ATOM 5870 O VAL C 218 38.847 46.396 −29.680 1.00 44.25 O ATOM 5871 CB VAL C 218 39.514 43.186 −29.279 1.00 38.50 C ATOM 5872 CG1 VAL C 218 38.038 43.421 −28.929 1.00 33.76 C ATOM 5873 CG2 VAL C 218 39.685 41.922 −30.113 1.00 27.73 C ATOM 5874 N ALA C 219 40.624 46.089 −28.349 1.00 36.78 N ATOM 5875 CA ALA C 219 40.391 47.308 −27.582 1.00 42.71 C ATOM 5876 C ALA C 219 40.583 48.557 −28.430 1.00 55.20 C ATOM 5877 O ALA C 219 39.790 49.495 −28.350 1.00 55.28 O ATOM 5878 CB ALA C 219 41.298 47.360 −26.367 1.00 42.30 C ATOM 5879 N LEU C 220 41.642 48.578 −29.232 1.00 49.23 N ATOM 5880 CA LEU C 220 41.881 49.710 −30.115 1.00 50.83 C ATOM 5881 C LEU C 220 40.700 49.889 −31.062 1.00 57.54 C ATOM 5882 O LEU C 220 40.248 51.008 −31.305 1.00 58.22 O ATOM 5883 CB LEU C 220 43.180 49.524 −30.894 1.00 48.29 C ATOM 5884 CG LEU C 220 44.432 49.670 −30.023 1.00 62.84 C ATOM 5885 CD1 LEU C 220 45.682 49.253 −30.775 1.00 48.37 C ATOM 5886 CD2 LEU C 220 44.565 51.098 −29.490 1.00 46.47 C ATOM 5887 N ARG C 221 40.191 48.777 −31.577 1.00 48.17 N ATOM 5888 CA ARG C 221 39.042 48.814 −32.467 1.00 52.10 C ATOM 5889 C ARG C 221 37.866 49.535 −31.812 1.00 57.31 C ATOM 5890 O ARG C 221 37.283 50.451 −32.386 1.00 55.56 O ATOM 5891 CB ARG C 221 38.639 47.398 −32.879 1.00 57.74 C ATOM 5892 CG ARG C 221 39.610 46.739 −33.846 1.00 61.91 C ATOM 5893 CD ARG C 221 39.497 47.342 −35.235 1.00 88.09 C ATOM 5894 NE ARG C 221 40.552 46.876 −36.134 1.00 112.26 N ATOM 5895 CZ ARG C 221 40.603 47.157 −37.434 1.00 125.08 C ATOM 5896 NH1 ARG C 221 39.654 47.897 −37.991 1.00 124.00 N ATOM 5897 NH2 ARG C 221 41.602 46.697 −38.179 1.00 118.41 N ATOM 5898 N VAL C 222 37.521 49.119 −30.601 1.00 61.88 N ATOM 5899 CA VAL C 222 36.419 49.740 −29.882 1.00 57.08 C ATOM 5900 C VAL C 222 36.595 51.254 −29.789 1.00 56.34 C ATOM 5901 O VAL C 222 35.620 52.001 −29.814 1.00 55.40 O ATOM 5902 CB VAL C 222 36.268 49.147 −28.481 1.00 42.21 C ATOM 5903 CG1 VAL C 222 35.170 49.859 −27.718 1.00 41.64 C ATOM 5904 CG2 VAL C 222 35.973 47.664 −28.583 1.00 45.93 C ATOM 5905 N TYR C 223 37.840 51.705 −29.695 1.00 61.23 N ATOM 5906 CA TYR C 223 38.118 53.136 −29.607 1.00 67.98 C ATOM 5907 C TYR C 223 37.758 53.850 −30.902 1.00 68.56 C ATOM 5908 O TYR C 223 37.087 54.880 −30.891 1.00 66.70 O ATOM 5909 CB TYR C 223 39.586 53.398 −29.274 1.00 62.43 C ATOM 5910 CG TYR C 223 39.871 54.846 −28.961 1.00 68.79 C ATOM 5911 CD1 TYR C 223 39.330 55.449 −27.833 1.00 74.33 C ATOM 5912 CD2 TYR C 223 40.681 55.613 −29.789 1.00 77.11 C ATOM 5913 CE1 TYR C 223 39.586 56.775 −27.535 1.00 87.02 C ATOM 5914 CE2 TYR C 223 40.945 56.944 −29.500 1.00 87.04 C ATOM 5915 CZ TYR C 223 40.392 57.520 −28.373 1.00 90.55 C ATOM 5916 OH TYR C 223 40.650 58.840 −28.081 1.00 93.20 O ATOM 5917 N ARG C 224 38.216 53.303 −32.020 1.00 65.33 N ATOM 5918 CA ARG C 224 37.915 53.891 −33.312 1.00 64.17 C ATOM 5919 C ARG C 224 36.412 53.928 −33.512 1.00 71.69 C ATOM 5920 O ARG C 224 35.871 54.916 −33.994 1.00 79.44 O ATOM 5921 CB ARG C 224 38.613 53.119 −34.433 1.00 62.48 C ATOM 5922 CG ARG C 224 40.113 53.378 −34.476 1.00 79.52 C ATOM 5923 CD ARG C 224 40.890 52.319 −35.248 1.00 88.95 C ATOM 5924 NE ARG C 224 42.317 52.396 −34.935 1.00 99.82 N ATOM 5925 CZ ARG C 224 43.277 51.779 −35.618 1.00 105.70 C ATOM 5926 NH1 ARG C 224 42.972 51.033 −36.670 1.00 105.31 N ATOM 5927 NH2 ARG C 224 44.545 51.916 −35.249 1.00 93.37 N ATOM 5928 N GLU C 225 35.742 52.856 −33.106 1.00 71.38 N ATOM 5929 CA GLU C 225 34.296 52.758 −33.239 1.00 71.79 C ATOM 5930 C GLU C 225 33.565 53.802 −32.418 1.00 71.27 C ATOM 5931 O GLU C 225 32.563 54.357 −32.857 1.00 84.13 O ATOM 5932 CB GLU C 225 33.813 51.363 −32.856 1.00 71.55 C ATOM 5933 CG GLU C 225 33.838 50.395 −34.014 1.00 84.21 C ATOM 5934 CD GLU C 225 33.035 50.903 −35.196 1.00 106.40 C ATOM 5935 OE1 GLU C 225 32.124 51.739 −34.982 1.00 107.57 O ATOM 5936 OE2 GLU C 225 33.315 50.468 −36.335 1.00 102.40 O ATOM 5937 N ALA C 226 34.062 54.064 −31.220 1.00 72.84 N ATOM 5938 CA ALA C 226 33.430 55.048 −30.356 1.00 83.74 C ATOM 5939 C ALA C 226 33.597 56.441 −30.954 1.00 89.71 C ATOM 5940 O ALA C 226 32.710 57.286 −30.833 1.00 89.70 O ATOM 5941 CB ALA C 226 34.015 54.982 −28.954 1.00 71.61 C ATOM 5942 N LYS C 227 34.736 56.663 −31.607 1.00 86.20 N ATOM 5943 CA LYS C 227 35.017 57.928 −32.279 1.00 79.31 C ATOM 5944 C LYS C 227 34.138 58.112 −33.515 1.00 90.45 C ATOM 5945 O LYS C 227 33.530 59.169 −33.698 1.00 89.07 O ATOM 5946 CB LYS C 227 36.490 58.006 −32.679 1.00 76.70 C ATOM 5947 CG LYS C 227 37.417 58.489 −31.581 1.00 86.70 C ATOM 5948 CD LYS C 227 38.803 58.815 −32.138 1.00 86.55 C ATOM 5949 CE LYS C 227 39.623 59.631 −31.144 1.00 101.09 C ATOM 5950 NZ LYS C 227 40.945 60.047 −31.698 1.00 92.85 N ATOM 5951 N GLU C 228 34.077 57.081 −34.358 1.00 90.18 N ATOM 5952 CA GLU C 228 33.220 57.086 −35.548 1.00 88.21 C ATOM 5953 C GLU C 228 31.756 57.252 −35.174 1.00 82.11 C ATOM 5954 O GLU C 228 30.889 57.266 −36.041 1.00 93.94 O ATOM 5955 CB GLU C 228 33.369 55.787 −36.347 1.00 90.73 C ATOM 5956 CG GLU C 228 34.662 55.646 −37.131 1.00 107.96 C ATOM 5957 CD GLU C 228 34.774 54.293 −37.824 1.00 119.01 C ATOM 5958 OE1 GLU C 228 33.820 53.901 −38.532 1.00 103.70 O ATOM 5959 OE2 GLU C 228 35.818 53.623 −37.661 1.00 121.96 O ATOM 5960 N GLN C 229 31.483 57.347 −33.879 1.00 94.36 N ATOM 5961 CA GLN C 229 30.129 57.577 −33.403 1.00 90.87 C ATOM 5962 C GLN C 229 29.949 59.025 −32.979 1.00 88.63 C ATOM 5963 O GLN C 229 28.853 59.573 −33.088 1.00 97.12 O ATOM 5964 CB GLN C 229 29.793 56.642 −32.237 1.00 86.76 C ATOM 5965 CG GLN C 229 29.355 55.250 −32.666 1.00 89.40 C ATOM 5966 CD GLN C 229 28.831 54.421 −31.509 1.00 98.76 C ATOM 5967 OE1 GLN C 229 28.113 53.440 −31.709 1.00 92.31 O ATOM 5968 NE2 GLN C 229 29.187 54.812 −30.289 1.00 99.18 N ATOM 5969 N ILE C 230 31.034 59.640 −32.516 1.00 80.71 N ATOM 5970 CA ILE C 230 30.984 60.947 −31.872 1.00 101.22 C ATOM 5971 C ILE C 230 31.932 60.924 −30.700 1.00 112.02 C ATOM 5972 O ILE C 230 33.142 61.110 −30.826 1.00 116.06 O ATOM 5973 CB ILE C 230 29.636 61.186 −31.186 1.00 118.06 C ATOM 5974 CG1 ILE C 230 29.711 62.438 −30.317 1.00 116.29 C ATOM 5975 CG2 ILE C 230 29.299 60.019 −30.255 1.00 114.50 C ATOM 5976 CD1 ILE C 230 29.230 62.205 −28.891 1.00 114.01 C ATOM 5977 N ARG C 267 27.114 59.218 −21.807 1.00 99.65 N ATOM 5978 CA ARG C 267 27.833 58.880 −20.590 1.00 98.46 C ATOM 5979 C ARG C 267 28.524 57.547 −20.806 1.00 103.69 C ATOM 5980 O ARG C 267 29.478 57.210 −20.108 1.00 94.85 O ATOM 5981 CB ARG C 267 26.862 58.752 −19.413 1.00 112.20 C ATOM 5982 CG ARG C 267 26.305 60.070 −18.893 1.00 135.87 C ATOM 5983 CD ARG C 267 27.291 60.785 −17.965 1.00 142.64 C ATOM 5984 NE ARG C 267 26.876 62.159 −17.678 1.00 155.72 N ATOM 5985 CZ ARG C 267 27.579 63.026 −16.953 1.00 140.45 C ATOM 5986 NH1 ARG C 267 28.744 62.668 −16.427 1.00 134.81 N ATOM 5987 NH2 ARG C 267 27.115 64.256 −16.751 1.00 113.67 N ATOM 5988 N GLU C 268 28.025 56.794 −21.784 1.00 114.18 N ATOM 5989 CA GLU C 268 28.515 55.449 −22.084 1.00 101.00 C ATOM 5990 C GLU C 268 30.014 55.429 −22.341 1.00 91.48 C ATOM 5991 O GLU C 268 30.678 54.409 −22.150 1.00 83.95 O ATOM 5992 CB GLU C 268 27.784 54.875 −23.300 1.00 105.34 C ATOM 5993 CG GLU C 268 26.265 54.967 −23.221 1.00 124.17 C ATOM 5994 CD GLU C 268 25.677 54.116 −22.106 1.00 136.24 C ATOM 5995 OE1 GLU C 268 26.426 53.315 −21.507 1.00 135.19 O ATOM 5996 OE2 GLU C 268 24.464 54.249 −21.833 1.00 120.57 O ATOM 5997 N HIS C 269 30.546 56.561 −22.780 1.00 85.84 N ATOM 5998 CA HIS C 269 31.967 56.659 −23.071 1.00 86.16 C ATOM 5999 C HIS C 269 32.824 56.707 −21.808 1.00 81.90 C ATOM 6000 O HIS C 269 33.910 56.128 −21.761 1.00 69.05 O ATOM 6001 CB HIS C 269 32.227 57.863 −23.966 1.00 90.42 C ATOM 6002 CG HIS C 269 31.768 57.658 −25.373 1.00 100.75 C ATOM 6003 ND1 HIS C 269 32.549 57.969 −26.465 1.00 102.38 N ATOM 6004 CD2 HIS C 269 30.619 57.139 −25.866 1.00 105.46 C ATOM 6005 CE1 HIS C 269 31.892 57.669 −27.571 1.00 103.19 C ATOM 6006 NE2 HIS C 269 30.719 57.163 −27.237 1.00 106.74 N ATOM 6007 N LYS C 270 32.335 57.398 −20.785 1.00 84.94 N ATOM 6008 CA LYS C 270 33.032 57.416 −19.509 1.00 84.11 C ATOM 6009 C LYS C 270 33.159 55.982 −19.017 1.00 74.02 C ATOM 6010 O LYS C 270 34.207 55.578 −18.520 1.00 66.77 O ATOM 6011 CB LYS C 270 32.293 58.292 −18.494 1.00 85.75 C ATOM 6012 CG LYS C 270 32.225 59.756 −18.909 1.00 109.03 C ATOM 6013 CD LYS C 270 31.214 60.548 −18.088 1.00 118.93 C ATOM 6014 CE LYS C 270 30.969 61.921 −18.702 1.00 115.36 C ATOM 6015 NZ LYS C 270 32.249 62.625 −19.018 1.00 117.95 N ATOM 6016 N ALA C 271 32.086 55.212 −19.182 1.00 76.50 N ATOM 6017 CA ALA C 271 32.092 53.799 −18.819 1.00 66.29 C ATOM 6018 C ALA C 271 33.120 53.057 −19.659 1.00 64.83 C ATOM 6019 O ALA C 271 33.917 52.280 −19.132 1.00 54.11 O ATOM 6020 CB ALA C 271 30.709 53.183 −18.995 1.00 52.24 C ATOM 6021 N LEU C 272 33.112 53.301 −20.965 1.00 58.84 N ATOM 6022 CA LEU C 272 34.102 52.677 −21.820 1.00 63.60 C ATOM 6023 C LEU C 272 35.496 53.097 −21.387 1.00 56.10 C ATOM 6024 O LEU C 272 36.380 52.255 −21.231 1.00 54.77 O ATOM 6025 CB LEU C 272 33.865 53.011 −23.295 1.00 74.65 C ATOM 6026 CG LEU C 272 32.661 52.337 −23.961 1.00 70.84 C ATOM 6027 CD1 LEU C 272 32.768 52.475 −25.467 1.00 56.81 C ATOM 6028 CD2 LEU C 272 32.553 50.871 −23.564 1.00 52.22 C ATOM 6029 N LYS C 273 35.684 54.395 −21.169 1.00 58.98 N ATOM 6030 CA LYS C 273 37.003 54.909 −20.818 1.00 60.29 C ATOM 6031 C LYS C 273 37.533 54.254 −19.547 1.00 56.92 C ATOM 6032 O LYS C 273 38.697 53.859 −19.486 1.00 54.15 O ATOM 6033 CB LYS C 273 36.995 56.430 −20.665 1.00 65.43 C ATOM 6034 CG LYS C 273 38.393 57.029 −20.758 1.00 67.27 C ATOM 6035 CD LYS C 273 38.513 58.349 −20.021 1.00 67.50 C ATOM 6036 CE LYS C 273 39.931 58.899 −20.147 1.00 75.82 C ATOM 6037 NZ LYS C 273 40.176 60.073 −19.254 1.00 91.27 N ATOM 6038 N THR C 274 36.678 54.143 −18.534 1.00 52.35 N ATOM 6039 CA THR C 274 37.051 53.457 −17.303 1.00 57.60 C ATOM 6040 C THR C 274 37.596 52.063 −17.608 1.00 51.69 C ATOM 6041 O THR C 274 38.625 51.670 −17.066 1.00 42.03 O ATOM 6042 CB THR C 274 35.863 53.336 −16.320 1.00 62.31 C ATOM 6043 OG1 THR C 274 35.598 54.610 −15.713 1.00 68.90 O ATOM 6044 CG2 THR C 274 36.177 52.327 −15.226 1.00 53.15 C ATOM 6045 N LEU C 275 36.911 51.329 −18.485 1.00 49.01 N ATOM 6046 CA LEU C 275 37.328 49.978 −18.845 1.00 40.47 C ATOM 6047 C LEU C 275 38.696 49.979 −19.500 1.00 42.43 C ATOM 6048 O LEU C 275 39.504 49.090 −19.252 1.00 50.74 O ATOM 6049 CB LEU C 275 36.312 49.308 −19.765 1.00 30.69 C ATOM 6050 CG LEU C 275 34.905 49.171 −19.191 1.00 42.31 C ATOM 6051 CD1 LEU C 275 33.971 48.475 −20.171 1.00 30.51 C ATOM 6052 CD2 LEU C 275 34.938 48.447 −17.854 1.00 37.83 C ATOM 6053 N GLY C 276 38.960 50.973 −20.336 1.00 40.24 N ATOM 6054 CA GLY C 276 40.251 51.078 −20.989 1.00 36.24 C ATOM 6055 C GLY C 276 41.340 51.364 −19.978 1.00 41.04 C ATOM 6056 O GLY C 276 42.476 50.938 −20.138 1.00 46.37 O ATOM 6057 N ILE C 277 40.986 52.087 −18.925 1.00 40.15 N ATOM 6058 CA ILE C 277 41.931 52.394 −17.864 1.00 44.60 C ATOM 6059 C ILE C 277 42.230 51.152 −17.011 1.00 46.43 C ATOM 6060 O ILE C 277 43.389 50.873 −16.695 1.00 47.86 O ATOM 6061 CB ILE C 277 41.425 53.558 −16.995 1.00 49.65 C ATOM 6062 CG1 ILE C 277 41.402 54.850 −17.816 1.00 42.71 C ATOM 6063 CG2 ILE C 277 42.295 53.726 −15.753 1.00 37.10 C ATOM 6064 CD1 ILE C 277 40.687 55.996 −17.136 1.00 46.73 C ATOM 6065 N ILE C 278 41.182 50.418 −16.641 1.00 41.13 N ATOM 6066 CA ILE C 278 41.320 49.106 −16.015 1.00 36.15 C ATOM 6067 C ILE C 278 42.344 48.271 −16.781 1.00 45.83 C ATOM 6068 O ILE C 278 43.257 47.669 −16.189 1.00 39.16 O ATOM 6069 CB ILE C 278 39.975 48.343 −16.031 1.00 35.12 C ATOM 6070 CG1 ILE C 278 38.957 49.018 −15.119 1.00 42.49 C ATOM 6071 CG2 ILE C 278 40.151 46.900 −15.627 1.00 38.87 C ATOM 6072 CD1 ILE C 278 39.539 49.551 −13.853 1.00 50.28 C ATOM 6073 N MET C 279 42.190 48.258 −18.103 1.00 36.04 N ATOM 6074 CA MET C 279 43.045 47.468 −18.986 1.00 42.61 C ATOM 6075 C MET C 279 44.471 48.001 −19.081 1.00 40.50 C ATOM 6076 O MET C 279 45.422 47.230 −19.022 1.00 47.57 O ATOM 6077 CB MET C 279 42.444 47.375 −20.396 1.00 40.96 C ATOM 6078 CG MET C 279 41.132 46.606 −20.485 1.00 41.77 C ATOM 6079 SD MET C 279 40.450 46.627 −22.161 1.00 67.30 S ATOM 6080 CE MET C 279 38.736 46.183 −21.854 1.00 41.57 C ATOM 6081 N GLY C 280 44.620 49.313 −19.234 1.00 36.86 N ATOM 6082 CA GLY C 280 45.933 49.908 −19.421 1.00 39.92 C ATOM 6083 C GLY C 280 46.789 49.807 −18.173 1.00 45.26 C ATOM 6084 O GLY C 280 47.995 49.534 −18.232 1.00 34.76 O ATOM 6085 N VAL C 281 46.151 50.034 −17.031 1.00 36.28 N ATOM 6086 CA VAL C 281 46.825 49.874 −15.762 1.00 37.13 C ATOM 6087 C VAL C 281 47.224 48.417 −15.590 1.00 37.96 C ATOM 6088 O VAL C 281 48.288 48.126 −15.060 1.00 39.33 O ATOM 6089 CB VAL C 281 45.947 50.328 −14.572 1.00 46.83 C ATOM 6090 CG1 VAL C 281 46.469 49.748 −13.266 1.00 37.96 C ATOM 6091 CG2 VAL C 281 45.889 51.842 −14.494 1.00 41.78 C ATOM 6092 N PHE C 282 46.379 47.495 −16.036 1.00 34.25 N ATOM 6093 CA PHE C 282 46.737 46.088 −15.913 1.00 30.73 C ATOM 6094 C PHE C 282 48.018 45.806 −16.685 1.00 43.33 C ATOM 6095 O PHE C 282 48.936 45.147 −16.181 1.00 44.86 O ATOM 6096 CB PHE C 282 45.632 45.165 −16.413 1.00 29.27 C ATOM 6097 CG PHE C 282 45.992 43.708 −16.332 1.00 34.08 C ATOM 6098 CD1 PHE C 282 45.641 42.953 −15.223 1.00 36.94 C ATOM 6099 CD2 PHE C 282 46.709 43.093 −17.355 1.00 36.74 C ATOM 6100 CE1 PHE C 282 45.982 41.609 −15.139 1.00 26.58 C ATOM 6101 CE2 PHE C 282 47.059 41.753 −17.272 1.00 28.78 C ATOM 6102 CZ PHE C 282 46.695 41.015 −16.165 1.00 23.99 C ATOM 6103 N THR C 283 48.078 46.310 −17.912 1.00 34.43 N ATOM 6104 CA THR C 283 49.193 46.021 −18.788 1.00 32.81 C ATOM 6105 C THR C 283 50.463 46.641 −18.241 1.00 40.24 C ATOM 6106 O THR C 283 51.537 46.049 −18.334 1.00 43.70 O ATOM 6107 CB THR C 283 48.932 46.536 −20.216 1.00 39.34 C ATOM 6108 OG1 THR C 283 47.731 45.942 −20.716 1.00 44.17 O ATOM 6109 CG2 THR C 283 50.095 46.186 −21.158 1.00 29.48 C ATOM 6110 N LEU C 284 50.337 47.837 −17.676 1.00 42.21 N ATOM 6111 CA LEU C 284 51.490 48.535 −17.125 1.00 46.01 C ATOM 6112 C LEU C 284 52.035 47.798 −15.910 1.00 43.39 C ATOM 6113 O LEU C 284 53.244 47.643 −15.763 1.00 45.88 O ATOM 6114 CB LEU C 284 51.113 49.972 −16.761 1.00 54.66 C ATOM 6115 CG LEU C 284 51.207 50.954 −17.927 1.00 62.95 C ATOM 6116 CD1 LEU C 284 50.289 52.168 −17.733 1.00 46.70 C ATOM 6117 CD2 LEU C 284 52.661 51.362 −18.110 1.00 54.16 C ATOM 6118 N CYS C 285 51.129 47.328 −15.058 1.00 34.31 N ATOM 6119 CA CYS C 285 51.496 46.664 −13.811 1.00 34.98 C ATOM 6120 C CYS C 285 52.076 45.264 −13.985 1.00 37.69 C ATOM 6121 O CYS C 285 52.842 44.807 −13.143 1.00 44.00 O ATOM 6122 CB CYS C 285 50.293 46.588 −12.868 1.00 39.48 C ATOM 6123 SG CYS C 285 49.730 48.177 −12.207 1.00 49.36 S ATOM 6124 N TRP C 286 51.710 44.576 −15.061 1.00 37.34 N ATOM 6125 CA TRP C 286 52.168 43.199 −15.261 1.00 32.71 C ATOM 6126 C TRP C 286 53.205 43.017 −16.356 1.00 32.80 C ATOM 6127 O TRP C 286 53.891 42.006 −16.400 1.00 39.79 O ATOM 6128 CB TRP C 286 50.994 42.278 −15.555 1.00 28.57 C ATOM 6129 CG TRP C 286 50.342 41.769 −14.346 1.00 25.42 C ATOM 6130 CD1 TRP C 286 49.094 42.053 −13.923 1.00 27.38 C ATOM 6131 CD2 TRP C 286 50.906 40.880 −13.378 1.00 26.93 C ATOM 6132 NE1 TRP C 286 48.830 41.392 −12.756 1.00 28.26 N ATOM 6133 CE2 TRP C 286 49.929 40.661 −12.398 1.00 24.74 C ATOM 6134 CE3 TRP C 286 52.149 40.251 −13.244 1.00 32.49 C ATOM 6135 CZ2 TRP C 286 50.147 39.842 −11.285 1.00 27.37 C ATOM 6136 CZ3 TRP C 286 52.371 39.436 −12.139 1.00 28.94 C ATOM 6137 CH2 TRP C 286 51.372 39.241 −11.173 1.00 28.95 C ATOM 6138 N LEU C 287 53.318 43.978 −17.252 1.00 30.59 N ATOM 6139 CA LEU C 287 54.184 43.771 −18.396 1.00 37.19 C ATOM 6140 C LEU C 287 55.659 43.711 −18.000 1.00 43.38 C ATOM 6141 O LEU C 287 56.378 42.823 −18.459 1.00 48.76 O ATOM 6142 CB LEU C 287 53.930 44.808 −19.498 1.00 33.25 C ATOM 6143 CG LEU C 287 54.582 44.476 −20.842 1.00 50.14 C ATOM 6144 CD1 LEU C 287 54.276 43.037 −21.293 1.00 42.55 C ATOM 6145 CD2 LEU C 287 54.150 45.484 −21.897 1.00 44.25 C ATOM 6146 N PRO C 288 56.120 44.644 −17.144 1.00 42.07 N ATOM 6147 CA PRO C 288 57.533 44.566 −16.752 1.00 44.53 C ATOM 6148 C PRO C 288 57.922 43.153 −16.335 1.00 41.31 C ATOM 6149 O PRO C 288 58.942 42.628 −16.799 1.00 40.08 O ATOM 6150 CB PRO C 288 57.620 45.525 −15.563 1.00 33.71 C ATOM 6151 CG PRO C 288 56.574 46.555 −15.856 1.00 38.66 C ATOM 6152 CD PRO C 288 55.445 45.810 −16.542 1.00 40.76 C ATOM 6153 N PHE C 289 57.099 42.541 −15.490 1.00 36.77 N ATOM 6154 CA PHE C 289 57.363 41.189 −15.011 1.00 36.16 C ATOM 6155 C PHE C 289 57.486 40.161 −16.141 1.00 38.33 C ATOM 6156 O PHE C 289 58.434 39.377 −16.167 1.00 41.88 O ATOM 6157 CB PHE C 289 56.295 40.762 −14.005 1.00 31.19 C ATOM 6158 CG PHE C 289 56.410 39.332 −13.566 1.00 30.45 C ATOM 6159 CD1 PHE C 289 57.195 38.985 −12.474 1.00 29.48 C ATOM 6160 CD2 PHE C 289 55.724 38.329 −14.240 1.00 31.94 C ATOM 6161 CE1 PHE C 289 57.302 37.665 −12.059 1.00 23.99 C ATOM 6162 CE2 PHE C 289 55.823 37.008 −13.833 1.00 27.89 C ATOM 6163 CZ PHE C 289 56.616 36.678 −12.740 1.00 27.06 C ATOM 6164 N PHE C 290 56.541 40.163 −17.076 1.00 35.54 N ATOM 6165 CA PHE C 290 56.595 39.199 −18.176 1.00 38.64 C ATOM 6166 C PHE C 290 57.701 39.479 −19.175 1.00 38.15 C ATOM 6167 O PHE C 290 58.231 38.545 −19.783 1.00 38.83 O ATOM 6168 CB PHE C 290 55.237 39.041 −18.860 1.00 33.36 C ATOM 6169 CG PHE C 290 54.264 38.276 −18.038 1.00 31.42 C ATOM 6170 CD1 PHE C 290 53.268 38.936 −17.332 1.00 31.11 C ATOM 6171 CD2 PHE C 290 54.381 36.899 −17.915 1.00 29.34 C ATOM 6172 CE1 PHE C 290 52.382 38.228 −16.546 1.00 30.33 C ATOM 6173 CE2 PHE C 290 53.505 36.178 −17.121 1.00 25.35 C ATOM 6174 CZ PHE C 290 52.502 36.837 −16.442 1.00 29.59 C ATOM 6175 N LEU C 291 58.054 40.752 −19.341 1.00 34.51 N ATOM 6176 CA LEU C 291 59.242 41.095 −20.117 1.00 37.90 C ATOM 6177 C LEU C 291 60.463 40.468 −19.455 1.00 47.61 C ATOM 6178 O LEU C 291 61.218 39.728 −20.097 1.00 38.90 O ATOM 6179 CB LEU C 291 59.434 42.605 −20.214 1.00 40.65 C ATOM 6180 CG LEU C 291 58.500 43.364 −21.152 1.00 58.43 C ATOM 6181 CD1 LEU C 291 59.184 44.642 −21.627 1.00 48.77 C ATOM 6182 CD2 LEU C 291 58.111 42.490 −22.336 1.00 36.08 C ATOM 6183 N VAL C 292 60.641 40.756 −18.163 1.00 41.33 N ATOM 6184 CA VAL C 292 61.796 40.262 −17.422 1.00 46.37 C ATOM 6185 C VAL C 292 61.837 38.739 −17.431 1.00 42.06 C ATOM 6186 O VAL C 292 62.900 38.130 −17.421 1.00 42.24 O ATOM 6187 CB VAL C 292 61.804 40.794 −15.975 1.00 48.73 C ATOM 6188 CG1 VAL C 292 62.638 39.897 −15.077 1.00 58.93 C ATOM 6189 CG2 VAL C 292 62.334 42.213 −15.945 1.00 49.23 C ATOM 6190 N ASN C 293 60.661 38.137 −17.468 1.00 45.58 N ATOM 6191 CA ASN C 293 60.545 36.692 −17.489 1.00 51.02 C ATOM 6192 C ASN C 293 61.188 36.079 −18.728 1.00 49.09 C ATOM 6193 O ASN C 293 61.848 35.040 −18.656 1.00 49.94 O ATOM 6194 CB ASN C 293 59.073 36.293 −17.421 1.00 49.15 C ATOM 6195 CG ASN C 293 58.870 34.957 −16.752 1.00 56.39 C ATOM 6196 OD1 ASN C 293 59.432 34.689 −15.684 1.00 53.12 O ATOM 6197 ND2 ASN C 293 58.067 34.102 −17.378 1.00 53.08 N ATOM 6198 N ILE C 294 60.993 36.722 −19.872 1.00 50.65 N ATOM 6199 CA ILE C 294 61.531 36.191 −21.119 1.00 48.96 C ATOM 6200 C ILE C 294 63.022 36.472 −21.274 1.00 40.86 C ATOM 6201 O ILE C 294 63.795 35.563 −21.581 1.00 36.11 O ATOM 6202 CB ILE C 294 60.771 36.725 −22.323 1.00 47.06 C ATOM 6203 CG1 ILE C 294 59.295 36.343 −22.214 1.00 42.91 C ATOM 6204 CG2 ILE C 294 61.368 36.164 −23.602 1.00 56.91 C ATOM 6205 CD1 ILE C 294 58.409 37.161 −23.117 1.00 48.12 C ATOM 6206 N VAL C 295 63.416 37.726 −21.055 1.00 40.67 N ATOM 6207 CA VAL C 295 64.826 38.099 −21.036 1.00 35.22 C ATOM 6208 C VAL C 295 65.647 37.060 −20.289 1.00 39.35 C ATOM 6209 O VAL C 295 66.676 36.617 −20.774 1.00 45.85 O ATOM 6210 CB VAL C 295 65.059 39.467 −20.376 1.00 32.86 C ATOM 6211 CG1 VAL C 295 66.518 39.619 −20.003 1.00 38.15 C ATOM 6212 CG2 VAL C 295 64.641 40.584 −21.304 1.00 27.14 C ATOM 6213 N ASN C 296 65.176 36.672 −19.110 1.00 39.32 N ATOM 6214 CA ASN C 296 65.838 35.655 −18.304 1.00 46.96 C ATOM 6215 C ASN C 296 66.082 34.332 −19.027 1.00 49.64 C ATOM 6216 O ASN C 296 67.129 33.702 −18.854 1.00 55.79 O ATOM 6217 CB ASN C 296 65.053 35.396 −17.015 1.00 49.24 C ATOM 6218 CG ASN C 296 65.811 35.818 −15.776 1.00 64.80 C ATOM 6219 OD1 ASN C 296 66.966 36.257 −15.848 1.00 65.41 O ATOM 6220 ND2 ASN C 296 65.167 35.683 −14.624 1.00 83.24 N ATOM 6221 N VAL C 297 65.108 33.899 −19.815 1.00 46.00 N ATOM 6222 CA VAL C 297 65.236 32.645 −20.537 1.00 55.34 C ATOM 6223 C VAL C 297 66.475 32.674 −21.435 1.00 61.06 C ATOM 6224 O VAL C 297 67.177 31.673 −21.583 1.00 49.34 O ATOM 6225 CB VAL C 297 63.981 32.356 −21.375 1.00 46.45 C ATOM 6226 CG1 VAL C 297 64.148 31.065 −22.159 1.00 44.51 C ATOM 6227 CG2 VAL C 297 62.762 32.277 −20.475 1.00 53.06 C ATOM 6228 N PHE C 298 66.746 33.841 −22.010 1.00 56.58 N ATOM 6229 CA PHE C 298 67.868 34.022 −22.919 1.00 60.95 C ATOM 6230 C PHE C 298 69.183 34.147 −22.164 1.00 65.01 C ATOM 6231 O PHE C 298 70.184 33.526 −22.523 1.00 79.89 O ATOM 6232 CB PHE C 298 67.643 35.269 −23.771 1.00 59.40 C ATOM 6233 CG PHE C 298 66.521 35.132 −24.759 1.00 61.55 C ATOM 6234 CD1 PHE C 298 65.654 34.053 −24.701 1.00 74.26 C ATOM 6235 CD2 PHE C 298 66.318 36.096 −25.731 1.00 85.59 C ATOM 6236 CE1 PHE C 298 64.616 33.923 −25.607 1.00 70.58 C ATOM 6237 CE2 PHE C 298 65.279 35.976 −26.639 1.00 95.91 C ATOM 6238 CZ PHE C 298 64.428 34.885 −26.576 1.00 82.51 C ATOM 6239 N ASN C 299 69.169 34.944 −21.105 1.00 62.91 N ATOM 6240 CA ASN C 299 70.381 35.272 −20.378 1.00 61.38 C ATOM 6241 C ASN C 299 70.134 35.434 −18.887 1.00 73.98 C ATOM 6242 O ASN C 299 69.970 36.560 −18.415 1.00 73.08 O ATOM 6243 CB ASN C 299 70.951 36.575 −20.928 1.00 71.52 C ATOM 6244 CG ASN C 299 72.221 36.992 −20.236 1.00 70.07 C ATOM 6245 OD1 ASN C 299 72.895 36.180 −19.606 1.00 78.04 O ATOM 6246 ND2 ASN C 299 72.566 38.263 −20.362 1.00 74.40 N ATOM 6247 N ARG C 300 70.095 34.318 −18.152 1.00 90.87 N ATOM 6248 CA ARG C 300 70.008 34.367 −16.690 1.00 70.01 C ATOM 6249 C ARG C 300 71.155 35.238 −16.216 1.00 73.77 C ATOM 6250 O ARG C 300 72.230 35.202 −16.802 1.00 93.16 O ATOM 6251 CB ARG C 300 70.121 32.966 −16.066 1.00 66.50 C ATOM 6252 CG ARG C 300 69.268 31.877 −16.744 1.00 92.81 C ATOM 6253 CD ARG C 300 68.842 30.762 −15.768 1.00 105.79 C ATOM 6254 NE ARG C 300 68.038 29.716 −16.413 1.00 113.60 N ATOM 6255 CZ ARG C 300 67.270 28.836 −15.766 1.00 110.73 C ATOM 6256 NH1 ARG C 300 67.179 28.861 −14.442 1.00 86.83 N ATOM 6257 NH2 ARG C 300 66.583 27.925 −16.447 1.00 102.03 N ATOM 6258 N ASP C 301 70.926 36.039 −15.182 1.00 79.53 N ATOM 6259 CA ASP C 301 71.980 36.881 −14.599 1.00 88.71 C ATOM 6260 C ASP C 301 72.269 38.173 −15.371 1.00 81.94 C ATOM 6261 O ASP C 301 73.365 38.719 −15.275 1.00 81.89 O ATOM 6262 CB ASP C 301 73.293 36.104 −14.434 1.00 83.67 C ATOM 6263 CG ASP C 301 73.095 34.732 −13.812 1.00 106.75 C ATOM 6264 OD1 ASP C 301 72.131 34.555 −13.031 1.00 109.74 O ATOM 6265 OD2 ASP C 301 73.917 33.833 −14.108 1.00 99.09 O ATOM 6266 N LEU C 302 71.301 38.658 −16.137 1.00 74.01 N ATOM 6267 CA LEU C 302 71.423 39.979 −16.738 1.00 72.68 C ATOM 6268 C LEU C 302 70.570 40.993 −15.982 1.00 89.27 C ATOM 6269 O LEU C 302 70.799 42.204 −16.066 1.00 90.09 O ATOM 6270 CB LEU C 302 70.986 39.969 −18.193 1.00 75.58 C ATOM 6271 CG LEU C 302 70.948 41.406 −18.708 1.00 70.89 C ATOM 6272 CD1 LEU C 302 72.366 41.871 −19.010 1.00 80.44 C ATOM 6273 CD2 LEU C 302 70.050 41.548 −19.921 1.00 74.40 C ATOM 6274 N VAL C 303 69.571 40.491 −15.262 1.00 85.01 N ATOM 6275 CA VAL C 303 68.719 41.334 −14.427 1.00 66.46 C ATOM 6276 C VAL C 303 68.571 40.718 −13.030 1.00 72.63 C ATOM 6277 O VAL C 303 68.351 39.508 −12.894 1.00 71.79 O ATOM 6278 CB VAL C 303 67.352 41.598 −15.099 1.00 74.75 C ATOM 6279 CG1 VAL C 303 66.311 42.030 −14.078 1.00 66.62 C ATOM 6280 CG2 VAL C 303 67.506 42.649 −16.190 1.00 77.61 C ATOM 6281 N PRO C 304 68.718 41.557 −11.988 1.00 65.84 N ATOM 6282 CA PRO C 304 68.854 41.175 −10.576 1.00 49.65 C ATOM 6283 C PRO C 304 67.594 40.600 −9.919 1.00 54.23 C ATOM 6284 O PRO C 304 66.540 41.241 −9.932 1.00 47.94 O ATOM 6285 CB PRO C 304 69.226 42.502 −9.911 1.00 41.78 C ATOM 6286 CG PRO C 304 68.629 43.521 −10.800 1.00 45.56 C ATOM 6287 CD PRO C 304 68.928 43.004 −12.160 1.00 56.24 C ATOM 6288 N ASP C 305 67.736 39.408 −9.335 1.00 55.16 N ATOM 6289 CA ASP C 305 66.670 38.718 −8.597 1.00 63.50 C ATOM 6290 C ASP C 305 65.721 39.633 −7.816 1.00 58.41 C ATOM 6291 O ASP C 305 64.517 39.376 −7.741 1.00 49.56 O ATOM 6292 CB ASP C 305 67.275 37.708 −7.611 1.00 74.46 C ATOM 6293 CG ASP C 305 67.573 36.358 −8.246 1.00 97.46 C ATOM 6294 OD1 ASP C 305 66.833 35.935 −9.161 1.00 97.26 O ATOM 6295 OD2 ASP C 305 68.547 35.707 −7.808 1.00 111.82 O ATOM 6296 N TRP C 306 66.269 40.676 −7.203 1.00 51.66 N ATOM 6297 CA TRP C 306 65.469 41.541 −6.354 1.00 49.78 C ATOM 6298 C TRP C 306 64.504 42.402 −7.168 1.00 46.94 C ATOM 6299 O TRP C 306 63.426 42.750 −6.690 1.00 47.32 O ATOM 6300 CB TRP C 306 66.370 42.417 −5.483 1.00 52.16 C ATOM 6301 CG TRP C 306 67.153 43.406 −6.263 1.00 50.19 C ATOM 6302 CD1 TRP C 306 68.449 43.287 −6.667 1.00 54.38 C ATOM 6303 CD2 TRP C 306 66.691 44.670 −6.752 1.00 44.18 C ATOM 6304 NE1 TRP C 306 68.825 44.403 −7.376 1.00 59.74 N ATOM 6305 CE2 TRP C 306 67.763 45.266 −7.445 1.00 51.21 C ATOM 6306 CE3 TRP C 306 65.474 45.352 −6.676 1.00 44.60 C ATOM 6307 CZ2 TRP C 306 67.659 46.515 −8.053 1.00 45.41 C ATOM 6308 CZ3 TRP C 306 65.369 46.592 −7.278 1.00 54.74 C ATOM 6309 CH2 TRP C 306 66.457 47.162 −7.959 1.00 55.43 C ATOM 6310 N LEU C 307 64.901 42.744 −8.392 1.00 42.95 N ATOM 6311 CA LEU C 307 64.054 43.508 −9.302 1.00 42.76 C ATOM 6312 C LEU C 307 63.013 42.582 −9.918 1.00 39.67 C ATOM 6313 O LEU C 307 61.913 42.989 −10.272 1.00 34.27 O ATOM 6314 CB LEU C 307 64.900 44.135 −10.402 1.00 48.73 C ATOM 6315 CG LEU C 307 64.128 44.887 −11.484 1.00 50.45 C ATOM 6316 CD1 LEU C 307 63.328 46.038 −10.887 1.00 44.45 C ATOM 6317 CD2 LEU C 307 65.079 45.386 −12.559 1.00 54.50 C ATOM 6318 N PHE C 308 63.385 41.320 −10.046 1.00 44.98 N ATOM 6319 CA PHE C 308 62.439 40.292 −10.408 1.00 42.10 C ATOM 6320 C PHE C 308 61.298 40.358 −9.393 1.00 35.26 C ATOM 6321 O PHE C 308 60.137 40.510 −9.750 1.00 37.60 O ATOM 6322 CB PHE C 308 63.135 38.928 −10.367 1.00 53.39 C ATOM 6323 CG PHE C 308 62.489 37.890 −11.229 1.00 61.90 C ATOM 6324 CD1 PHE C 308 62.831 37.775 −12.564 1.00 59.56 C ATOM 6325 CD2 PHE C 308 61.539 37.022 −10.701 1.00 76.20 C ATOM 6326 CE1 PHE C 308 62.231 36.822 −13.367 1.00 67.42 C ATOM 6327 CE2 PHE C 308 60.936 36.061 −11.499 1.00 76.53 C ATOM 6328 CZ PHE C 308 61.284 35.964 −12.836 1.00 66.84 C ATOM 6329 N VAL C 309 61.643 40.276 −8.117 1.00 44.16 N ATOM 6330 CA VAL C 309 60.649 40.339 −7.047 1.00 48.42 C ATOM 6331 C VAL C 309 59.876 41.665 −7.017 1.00 41.97 C ATOM 6332 O VAL C 309 58.642 41.672 −6.901 1.00 36.14 O ATOM 6333 CB VAL C 309 61.287 40.042 −5.673 1.00 45.87 C ATOM 6334 CG1 VAL C 309 60.322 40.362 −4.549 1.00 49.31 C ATOM 6335 CG2 VAL C 309 61.706 38.586 −5.601 1.00 36.42 C ATOM 6336 N ALA C 310 60.601 42.777 −7.127 1.00 41.28 N ATOM 6337 CA ALA C 310 59.987 44.107 −7.217 1.00 40.66 C ATOM 6338 C ALA C 310 58.847 44.135 −8.226 1.00 37.77 C ATOM 6339 O ALA C 310 57.735 44.556 −7.908 1.00 26.79 O ATOM 6340 CB ALA C 310 61.024 45.145 −7.590 1.00 33.14 C ATOM 6341 N PHE C 311 59.138 43.682 −9.443 1.00 34.24 N ATOM 6342 CA PHE C 311 58.153 43.681 −10.523 1.00 33.84 C ATOM 6343 C PHE C 311 56.940 42.767 −10.273 1.00 30.30 C ATOM 6344 O PHE C 311 55.817 43.099 −10.642 1.00 26.32 O ATOM 6345 CB PHE C 311 58.823 43.342 −11.862 1.00 31.50 C ATOM 6346 CG PHE C 311 59.509 44.515 −12.514 1.00 36.43 C ATOM 6347 CD1 PHE C 311 60.598 44.320 −13.355 1.00 35.51 C ATOM 6348 CD2 PHE C 311 59.071 45.815 −12.275 1.00 32.14 C ATOM 6349 CE1 PHE C 311 61.230 45.401 −13.953 1.00 45.19 C ATOM 6350 CE2 PHE C 311 59.696 46.900 −12.869 1.00 34.05 C ATOM 6351 CZ PHE C 311 60.776 46.698 −13.709 1.00 44.86 C ATOM 6352 N ASN C 312 57.165 41.620 −9.648 1.00 28.20 N ATOM 6353 CA ASN C 312 56.065 40.725 −9.342 1.00 27.13 C ATOM 6354 C ASN C 312 55.109 41.352 −8.306 1.00 32.75 C ATOM 6355 O ASN C 312 53.899 41.110 −8.334 1.00 30.23 O ATOM 6356 CB ASN C 312 56.612 39.372 −8.871 1.00 23.33 C ATOM 6357 CG ASN C 312 55.554 38.274 −8.849 1.00 28.58 C ATOM 6358 OD1 ASN C 312 55.873 37.104 −8.641 1.00 27.91 O ATOM 6359 ND2 ASN C 312 54.295 38.644 −9.052 1.00 35.12 N ATOM 6360 N TRP C 313 55.649 42.167 −7.401 1.00 31.63 N ATOM 6361 CA TRP C 313 54.820 42.885 −6.427 1.00 29.87 C ATOM 6362 C TRP C 313 54.049 44.051 −7.046 1.00 27.76 C ATOM 6363 O TRP C 313 53.008 44.470 −6.532 1.00 27.77 O ATOM 6364 CB TRP C 313 55.647 43.334 −5.209 1.00 27.90 C ATOM 6365 CG TRP C 313 55.798 42.231 −4.224 1.00 30.93 C ATOM 6366 CD1 TRP C 313 56.776 41.281 −4.199 1.00 34.09 C ATOM 6367 CD2 TRP C 313 54.904 41.914 −3.155 1.00 29.65 C ATOM 6368 NE1 TRP C 313 56.557 40.404 −3.164 1.00 30.84 N ATOM 6369 CE2 TRP C 313 55.410 40.771 −2.512 1.00 33.11 C ATOM 6370 CE3 TRP C 313 53.728 42.488 −2.677 1.00 27.25 C ATOM 6371 CZ2 TRP C 313 54.782 40.200 −1.414 1.00 34.75 C ATOM 6372 CZ3 TRP C 313 53.110 41.919 −1.587 1.00 29.79 C ATOM 6373 CH2 TRP C 313 53.636 40.792 −0.966 1.00 32.30 C ATOM 6374 N LEU C 314 54.569 44.568 −8.153 1.00 25.04 N ATOM 6375 CA LEU C 314 53.854 45.559 −8.929 1.00 26.40 C ATOM 6376 C LEU C 314 52.647 44.889 −9.586 1.00 31.77 C ATOM 6377 O LEU C 314 51.585 45.486 −9.717 1.00 31.16 O ATOM 6378 CB LEU C 314 54.771 46.162 −9.987 1.00 24.36 C ATOM 6379 CG LEU C 314 54.045 47.206 −10.830 1.00 27.12 C ATOM 6380 CD1 LEU C 314 53.487 48.304 −9.939 1.00 29.73 C ATOM 6381 CD2 LEU C 314 54.971 47.784 −11.865 1.00 31.44 C ATOM 6382 N GLY C 315 52.815 43.635 −9.991 1.00 31.34 N ATOM 6383 CA GLY C 315 51.706 42.864 −10.507 1.00 25.48 C ATOM 6384 C GLY C 315 50.670 42.599 −9.433 1.00 26.89 C ATOM 6385 O GLY C 315 49.471 42.680 −9.678 1.00 29.28 O ATOM 6386 N TYR C 316 51.136 42.267 −8.234 1.00 29.58 N ATOM 6387 CA TYR C 316 50.237 41.995 −7.119 1.00 34.76 C ATOM 6388 C TYR C 316 49.427 43.225 −6.732 1.00 37.34 C ATOM 6389 O TYR C 316 48.247 43.117 −6.403 1.00 39.83 O ATOM 6390 CB TYR C 316 51.012 41.529 −5.895 1.00 36.25 C ATOM 6391 CG TYR C 316 51.539 40.118 −5.958 1.00 35.61 C ATOM 6392 CD1 TYR C 316 52.636 39.745 −5.191 1.00 32.49 C ATOM 6393 CD2 TYR C 316 50.943 39.157 −6.768 1.00 31.64 C ATOM 6394 CE1 TYR C 316 53.128 38.464 −5.225 1.00 37.76 C ATOM 6395 CE2 TYR C 316 51.435 37.860 −6.814 1.00 35.73 C ATOM 6396 CZ TYR C 316 52.534 37.525 −6.038 1.00 38.35 C ATOM 6397 OH TYR C 316 53.056 36.258 −6.048 1.00 33.92 O ATOM 6398 N ALA C 317 50.072 44.388 −6.752 1.00 41.70 N ATOM 6399 CA ALA C 317 49.429 45.640 −6.350 1.00 44.41 C ATOM 6400 C ALA C 317 48.274 46.025 −7.276 1.00 36.59 C ATOM 6401 O ALA C 317 47.293 46.624 −6.843 1.00 39.89 O ATOM 6402 CB ALA C 317 50.460 46.772 −6.258 1.00 30.43 C ATOM 6403 N ASN C 318 48.394 45.682 −8.549 1.00 27.70 N ATOM 6404 CA ASN C 318 47.294 45.875 −9.471 1.00 37.90 C ATOM 6405 C ASN C 318 45.962 45.489 −8.817 1.00 36.19 C ATOM 6406 O ASN C 318 44.959 46.167 −8.998 1.00 43.02 O ATOM 6407 CB ASN C 318 47.524 45.047 −10.737 1.00 44.12 C ATOM 6408 CG ASN C 318 46.468 45.287 −11.798 1.00 44.49 C ATOM 6409 OD1 ASN C 318 46.524 46.280 −12.531 1.00 43.13 O ATOM 6410 ND2 ASN C 318 45.502 44.367 −11.896 1.00 32.86 N ATOM 6411 N SER C 319 45.961 44.407 −8.047 1.00 29.61 N ATOM 6412 CA SER C 319 44.733 43.894 −7.448 1.00 31.50 C ATOM 6413 C SER C 319 44.035 44.889 −6.533 1.00 41.64 C ATOM 6414 O SER C 319 42.878 44.683 −6.156 1.00 39.95 O ATOM 6415 CB SER C 319 45.004 42.616 −6.669 1.00 32.77 C ATOM 6416 OG SER C 319 45.209 41.533 −7.545 1.00 38.85 O ATOM 6417 N ALA C 320 44.732 45.962 −6.172 1.00 42.38 N ATOM 6418 CA ALA C 320 44.130 46.982 −5.323 1.00 40.79 C ATOM 6419 C ALA C 320 43.740 48.234 −6.111 1.00 42.66 C ATOM 6420 O ALA C 320 43.017 49.094 −5.612 1.00 48.99 O ATOM 6421 CB ALA C 320 45.054 47.331 −4.176 1.00 36.59 C ATOM 6422 N MET C 321 44.204 48.328 −7.348 1.00 38.55 N ATOM 6423 CA MET C 321 43.937 49.512 −8.159 1.00 47.66 C ATOM 6424 C MET C 321 42.516 49.603 −8.718 1.00 45.04 C ATOM 6425 O MET C 321 41.990 50.699 −8.898 1.00 48.89 O ATOM 6426 CB MET C 321 44.980 49.641 −9.267 1.00 40.75 C ATOM 6427 CG MET C 321 46.356 49.919 −8.703 1.00 49.11 C ATOM 6428 SD MET C 321 47.714 49.696 −9.856 1.00 60.69 S ATOM 6429 CE MET C 321 49.137 49.802 −8.741 1.00 42.22 C ATOM 6430 N ASN C 322 41.894 48.459 −8.976 1.00 50.35 N ATOM 6431 CA ASN C 322 40.553 48.436 −9.556 1.00 50.38 C ATOM 6432 C ASN C 322 39.507 49.217 −8.771 1.00 52.89 C ATOM 6433 O ASN C 322 38.892 50.138 −9.309 1.00 52.50 O ATOM 6434 CB ASN C 322 40.070 47.002 −9.757 1.00 54.32 C ATOM 6435 CG ASN C 322 40.511 46.435 −11.067 1.00 60.06 C ATOM 6436 OD1 ASN C 322 41.326 47.041 −11.765 1.00 40.84 O ATOM 6437 ND2 ASN C 322 39.973 45.268 −11.423 1.00 61.97 N ATOM 6438 N PRO C 323 39.283 48.838 −7.501 1.00 52.30 N ATOM 6439 CA PRO C 323 38.245 49.538 −6.747 1.00 51.33 C ATOM 6440 C PRO C 323 38.534 51.027 −6.711 1.00 47.59 C ATOM 6441 O PRO C 323 37.605 51.818 −6.834 1.00 50.18 O ATOM 6442 CB PRO C 323 38.348 48.915 −5.351 1.00 46.35 C ATOM 6443 CG PRO C 323 38.894 47.547 −5.601 1.00 45.73 C ATOM 6444 CD PRO C 323 39.892 47.753 −6.710 1.00 51.47 C ATOM 6445 N ILE C 324 39.803 51.401 −6.579 1.00 44.72 N ATOM 6446 CA ILE C 324 40.183 52.809 −6.646 1.00 51.59 C ATOM 6447 C ILE C 324 39.725 53.453 −7.951 1.00 53.69 C ATOM 6448 O ILE C 324 39.089 54.502 −7.941 1.00 59.30 O ATOM 6449 CB ILE C 324 41.700 53.002 −6.524 1.00 53.74 C ATOM 6450 CG1 ILE C 324 42.127 52.925 −5.056 1.00 52.85 C ATOM 6451 CG2 ILE C 324 42.118 54.334 −7.157 1.00 37.38 C ATOM 6452 CD1 ILE C 324 43.607 52.669 −4.878 1.00 60.65 C ATOM 6453 N ILE C 325 40.053 52.824 −9.074 1.00 51.40 N ATOM 6454 CA ILE C 325 39.695 53.364 −10.381 1.00 49.51 C ATOM 6455 C ILE C 325 38.178 53.507 −10.543 1.00 58.09 C ATOM 6456 O ILE C 325 37.694 54.471 −11.135 1.00 49.44 O ATOM 6457 CB ILE C 325 40.260 52.495 −11.527 1.00 49.16 C ATOM 6458 CG1 ILE C 325 41.779 52.411 −11.431 1.00 43.52 C ATOM 6459 CG2 ILE C 325 39.864 53.054 −12.887 1.00 49.11 C ATOM 6460 CD1 ILE C 325 42.426 51.844 −12.667 1.00 40.91 C ATOM 6461 N TYR C 326 37.426 52.553 −10.009 1.00 57.77 N ATOM 6462 CA TYR C 326 35.977 52.608 −10.118 1.00 58.32 C ATOM 6463 C TYR C 326 35.394 53.863 −9.470 1.00 60.88 C ATOM 6464 O TYR C 326 34.243 54.207 −9.712 1.00 55.76 O ATOM 6465 CB TYR C 326 35.338 51.358 −9.519 1.00 49.71 C ATOM 6466 CG TYR C 326 35.655 50.085 −10.265 1.00 55.77 C ATOM 6467 CD1 TYR C 326 35.747 48.873 −9.591 1.00 55.96 C ATOM 6468 CD2 TYR C 326 35.872 50.094 −11.644 1.00 54.13 C ATOM 6469 CE1 TYR C 326 36.031 47.702 −10.264 1.00 54.31 C ATOM 6470 CE2 TYR C 326 36.162 48.926 −12.330 1.00 51.16 C ATOM 6471 CZ TYR C 326 36.241 47.731 −11.631 1.00 52.74 C ATOM 6472 OH TYR C 326 36.530 46.556 −12.285 1.00 41.98 O ATOM 6473 N CYS C 327 36.194 54.544 −8.655 1.00 62.46 N ATOM 6474 CA CYS C 327 35.757 55.773 −7.989 1.00 67.59 C ATOM 6475 C CYS C 327 35.490 56.909 −8.972 1.00 74.14 C ATOM 6476 O CYS C 327 35.104 58.007 −8.571 1.00 78.91 O ATOM 6477 CB CYS C 327 36.791 56.229 −6.958 1.00 61.95 C ATOM 6478 SG CYS C 327 36.960 55.148 −5.520 1.00 66.64 S ATOM 6479 N ARG C 328 35.709 56.653 −10.256 1.00 70.02 N ATOM 6480 CA ARG C 328 35.417 57.649 −11.279 1.00 72.23 C ATOM 6481 C ARG C 328 33.912 57.799 −11.460 1.00 82.47 C ATOM 6482 O ARG C 328 33.416 58.888 −11.750 1.00 96.14 O ATOM 6483 CB ARG C 328 36.061 57.261 −12.608 1.00 70.19 C ATOM 6484 CG ARG C 328 37.518 57.660 −12.746 1.00 71.53 C ATOM 6485 CD ARG C 328 38.093 57.029 −13.989 1.00 62.36 C ATOM 6486 NE ARG C 328 37.070 56.919 −15.021 1.00 62.38 N ATOM 6487 CZ ARG C 328 37.013 57.695 −16.096 1.00 75.27 C ATOM 6488 NH1 ARG C 328 37.933 58.635 −16.283 1.00 76.75 N ATOM 6489 NH2 ARG C 328 36.041 57.528 −16.988 1.00 75.44 N ATOM 6490 N SER C 329 33.189 56.697 −11.283 1.00 86.41 N ATOM 6491 CA SER C 329 31.749 56.675 −11.519 1.00 87.97 C ATOM 6492 C SER C 329 30.988 57.335 −10.380 1.00 89.08 C ATOM 6493 O SER C 329 31.348 57.187 −9.214 1.00 73.68 O ATOM 6494 CB SER C 329 31.255 55.239 −11.721 1.00 91.47 C ATOM 6495 OG SER C 329 29.872 55.211 −12.026 1.00 78.47 O ATOM 6496 C16 PDL C 400 57.280 31.530 −16.048 1.00 48.57 C ATOM 6497 N3 PDL C 400 58.322 31.155 −16.325 1.00 40.11 N ATOM 6498 N1 PDL C 400 54.713 31.580 −16.545 1.00 44.31 N ATOM 6499 C1 PDL C 400 55.943 31.977 −15.752 1.00 46.12 C ATOM 6500 C2 PDL C 400 55.507 32.968 −14.687 1.00 32.90 C ATOM 6501 C3 PDL C 400 54.028 33.125 −14.796 1.00 28.37 C ATOM 6502 C4 PDL C 400 53.008 33.944 −14.009 1.00 28.86 C ATOM 6503 C5 PDL C 400 51.521 33.904 −14.358 1.00 34.03 C ATOM 6504 C6 PDL C 400 51.053 33.025 −15.526 1.00 31.57 C ATOM 6505 C7 PDL C 400 52.053 32.203 −16.319 1.00 21.76 C ATOM 6506 C8 PDL C 400 53.539 32.264 −15.955 1.00 31.07 C ATOM 6507 O1 PDL C 400 53.447 34.772 −12.978 1.00 39.15 O ATOM 6508 C9 PDL C 400 52.668 34.964 −11.833 1.00 36.42 C ATOM 6509 C10 PDL C 400 53.617 35.479 −10.745 1.00 29.67 C ATOM 6510 O2 PDL C 400 52.918 36.329 −9.865 1.00 37.36 O ATOM 6511 C11 PDL C 400 54.253 34.287 −10.010 1.00 30.49 C ATOM 6512 N2 PDL C 400 54.979 34.620 −8.778 1.00 26.38 N ATOM 6513 C12 PDL C 400 55.824 33.468 −8.414 1.00 31.75 C ATOM 6514 C13 PDL C 400 57.094 33.491 −9.314 1.00 19.60 C ATOM 6515 C14 PDL C 400 55.087 32.110 −8.630 1.00 21.33 C ATOM 6516 C15 PDL C 400 56.168 33.605 −6.908 1.00 29.02 C ATOM 6517 NA NA C 401 61.282 23.554 −2.478 1.00 37.52 Na

TABLE D CRYST1  55.500  86.800  95.500  67.60  73.30  85.80 P 1 SCALE1   0.018018 −0.001323 −0.005298    0.00000 SCALE2   0.000000  0.011552 −0.004700    0.00000 SCALE3   0.000000  0.000000  0.011803    0.00000 ATOM 6518 N GLU D 33 32.936 12.310 −58.825 1.00 70.87 N ATOM 6519 CA GLU D 33 32.400 11.204 −58.046 1.00 67.67 C ATOM 6520 C GLU D 33 33.262 9.953 −58.194 1.00 63.61 C ATOM 6521 O GLU D 33 33.563 9.283 −57.206 1.00 56.75 O ATOM 6522 CB GLU D 33 30.956 10.915 −58.442 1.00 59.28 C ATOM 6523 CG GLU D 33 30.241 10.019 −57.452 1.00 80.84 C ATOM 6524 CD GLU D 33 28.927 9.491 −57.985 1.00 95.18 C ATOM 6525 OE1 GLU D 33 28.516 9.909 −59.092 1.00 100.08 O ATOM 6526 OE2 GLU D 33 28.309 8.652 −57.294 1.00 85.89 O ATOM 6527 N ALA D 34 33.652 9.634 −59.426 1.00 61.18 N ATOM 6528 CA ALA D 34 34.650 8.600 −59.641 1.00 55.63 C ATOM 6529 C ALA D 34 35.905 9.021 −58.883 1.00 56.94 C ATOM 6530 O ALA D 34 36.497 8.231 −58.141 1.00 51.45 O ATOM 6531 CB ALA D 34 34.945 8.428 −61.119 1.00 33.86 C ATOM 6532 N GLY D 35 36.295 10.280 −59.056 1.00 51.21 N ATOM 6533 CA GLY D 35 37.450 10.820 −58.357 1.00 53.13 C ATOM 6534 C GLY D 35 37.378 10.669 −56.846 1.00 49.57 C ATOM 6535 O GLY D 35 38.199 9.989 −56.236 1.00 44.13 O ATOM 6536 N MET D 36 36.388 11.304 −56.233 1.00 56.71 N ATOM 6537 CA MET D 36 36.237 11.211 −54.788 1.00 45.41 C ATOM 6538 C MET D 36 36.219 9.760 −54.314 1.00 44.98 C ATOM 6539 O MET D 36 36.895 9.410 −53.353 1.00 47.98 O ATOM 6540 CB MET D 36 34.994 11.969 −54.321 1.00 51.72 C ATOM 6541 CG MET D 36 35.112 13.489 −54.472 1.00 67.06 C ATOM 6542 SD MET D 36 36.558 14.224 −53.653 1.00 85.95 S ATOM 6543 CE MET D 36 37.873 14.004 −54.865 1.00 55.31 C ATOM 6544 N SER D 37 35.459 8.915 −55.001 1.00 46.54 N ATOM 6545 CA SER D 37 35.384 7.499 −54.659 1.00 43.19 C ATOM 6546 C SER D 37 36.760 6.834 −54.607 1.00 40.39 C ATOM 6547 O SER D 37 37.055 6.062 −53.687 1.00 30.12 O ATOM 6548 CB SER D 37 34.481 6.754 −55.645 1.00 45.51 C ATOM 6549 OG SER D 37 33.127 7.117 −55.460 1.00 49.21 O ATOM 6550 N LEU D 38 37.595 7.121 −55.600 1.00 33.21 N ATOM 6551 CA LEU D 38 38.911 6.508 −55.653 1.00 38.92 C ATOM 6552 C LEU D 38 39.798 7.011 −54.500 1.00 44.71 C ATOM 6553 O LEU D 38 40.376 6.217 −53.741 1.00 34.90 O ATOM 6554 CB LEU D 38 39.573 6.751 −57.007 1.00 32.16 C ATOM 6555 CG LEU D 38 40.888 6.005 −57.200 1.00 38.54 C ATOM 6556 CD1 LEU D 38 40.674 4.490 −57.182 1.00 38.61 C ATOM 6557 CD2 LEU D 38 41.544 6.443 −58.483 1.00 37.96 C ATOM 6558 N LEU D 39 39.896 8.328 −54.363 1.00 34.73 N ATOM 6559 CA LEU D 39 40.613 8.909 −53.235 1.00 41.35 C ATOM 6560 C LEU D 39 40.246 8.249 −51.893 1.00 39.85 C ATOM 6561 O LEU D 39 41.123 7.917 −51.099 1.00 37.81 O ATOM 6562 CB LEU D 39 40.367 10.418 −53.152 1.00 46.88 C ATOM 6563 CG LEU D 39 41.128 11.131 −52.029 1.00 42.29 C ATOM 6564 CD1 LEU D 39 42.630 11.197 −52.335 1.00 37.23 C ATOM 6565 CD2 LEU D 39 40.559 12.524 −51.800 1.00 51.38 C ATOM 6566 N MET D 40 38.956 8.056 −51.644 1.00 35.09 N ATOM 6567 CA MET D 40 38.503 7.427 −50.406 1.00 28.75 C ATOM 6568 C MET D 40 38.929 5.966 −50.266 1.00 32.63 C ATOM 6569 O MET D 40 39.318 5.542 −49.191 1.00 32.67 O ATOM 6570 CB MET D 40 36.983 7.567 −50.244 1.00 40.54 C ATOM 6571 CG MET D 40 36.493 9.015 −50.079 1.00 55.55 C ATOM 6572 SD MET D 40 37.179 9.921 −48.656 1.00 81.76 S ATOM 6573 CE MET D 40 38.693 10.617 −49.329 1.00 44.42 C ATOM 6574 N ALA D 41 38.869 5.191 −51.345 1.00 42.14 N ATOM 6575 CA ALA D 41 39.361 3.818 −51.301 1.00 29.34 C ATOM 6576 C ALA D 41 40.883 3.802 −51.154 1.00 37.62 C ATOM 6577 O ALA D 41 41.483 2.761 −50.894 1.00 37.37 O ATOM 6578 CB ALA D 41 38.942 3.070 −52.549 1.00 35.84 C ATOM 6579 N LEU D 42 41.502 4.969 −51.305 1.00 35.43 N ATOM 6580 CA LEU D 42 42.958 5.082 −51.316 1.00 35.07 C ATOM 6581 C LEU D 42 43.597 5.793 −50.102 1.00 36.06 C ATOM 6582 O LEU D 42 44.818 5.680 −49.923 1.00 31.94 O ATOM 6583 CB LEU D 42 43.415 5.765 −52.625 1.00 43.14 C ATOM 6584 CG LEU D 42 44.198 5.014 −53.720 1.00 32.16 C ATOM 6585 CD1 LEU D 42 44.049 3.520 −53.616 1.00 28.71 C ATOM 6586 CD2 LEU D 42 43.793 5.481 −55.092 1.00 24.33 C ATOM 6587 N VAL D 43 42.807 6.514 −49.290 1.00 27.82 N ATOM 6588 CA VAL D 43 43.364 7.382 −48.219 1.00 30.44 C ATOM 6589 C VAL D 43 44.268 6.738 −47.181 1.00 31.15 C ATOM 6590 O VAL D 43 45.344 7.257 −46.915 1.00 31.06 O ATOM 6591 CB VAL D 43 42.309 8.167 −47.393 1.00 30.55 C ATOM 6592 CG1 VAL D 43 42.385 9.663 −47.694 1.00 33.24 C ATOM 6593 CG2 VAL D 43 40.911 7.590 −47.567 1.00 44.75 C ATOM 6594 N VAL D 44 43.821 5.652 −46.552 1.00 28.40 N ATOM 6595 CA VAL D 44 44.656 5.004 −45.547 1.00 26.07 C ATOM 6596 C VAL D 44 46.028 4.706 −46.122 1.00 32.39 C ATOM 6597 O VAL D 44 47.048 4.985 −45.488 1.00 34.61 O ATOM 6598 CB VAL D 44 44.038 3.720 −45.000 1.00 30.89 C ATOM 6599 CG1 VAL D 44 45.029 3.005 −44.085 1.00 19.55 C ATOM 6600 CG2 VAL D 44 42.753 4.036 −44.253 1.00 31.89 C ATOM 6601 N LEU D 45 46.051 4.155 −47.332 1.00 34.18 N ATOM 6602 CA LEU D 45 47.310 3.907 −48.023 1.00 33.44 C ATOM 6603 C LEU D 45 48.062 5.218 −48.276 1.00 34.22 C ATOM 6604 O LEU D 45 49.210 5.369 −47.850 1.00 33.31 O ATOM 6605 CB LEU D 45 47.079 3.152 −49.342 1.00 29.70 C ATOM 6606 CG LEU D 45 48.343 2.980 −50.196 1.00 34.73 C ATOM 6607 CD1 LEU D 45 49.286 1.896 −49.644 1.00 23.71 C ATOM 6608 CD2 LEU D 45 47.969 2.703 −51.636 1.00 33.78 C ATOM 6609 N LEU D 46 47.404 6.157 −48.958 1.00 29.97 N ATOM 6610 CA LEU D 46 47.993 7.460 −49.289 1.00 32.71 C ATOM 6611 C LEU D 46 48.594 8.243 −48.110 1.00 37.56 C ATOM 6612 O LEU D 46 49.624 8.908 −48.260 1.00 40.65 O ATOM 6613 CB LEU D 46 46.966 8.338 −50.002 1.00 31.94 C ATOM 6614 CG LEU D 46 46.673 8.005 −51.457 1.00 37.27 C ATOM 6615 CD1 LEU D 46 45.775 9.073 −52.071 1.00 37.01 C ATOM 6616 CD2 LEU D 46 47.976 7.900 −52.211 1.00 28.57 C ATOM 6617 N ILE D 47 47.934 8.189 −46.956 1.00 33.73 N ATOM 6618 CA ILE D 47 48.418 8.881 −45.765 1.00 36.23 C ATOM 6619 C ILE D 47 49.607 8.147 −45.149 1.00 37.47 C ATOM 6620 O ILE D 47 50.623 8.764 −44.840 1.00 31.91 O ATOM 6621 CB ILE D 47 47.308 9.055 −44.688 1.00 31.27 C ATOM 6622 CG1 ILE D 47 46.215 10.005 −45.172 1.00 32.52 C ATOM 6623 CG2 ILE D 47 47.888 9.587 −43.413 1.00 25.53 C ATOM 6624 CD1 ILE D 47 44.922 9.909 −44.370 1.00 28.45 C ATOM 6625 N VAL D 48 49.473 6.830 −44.978 1.00 42.08 N ATOM 6626 CA VAL D 48 50.486 6.021 −44.286 1.00 32.68 C ATOM 6627 C VAL D 48 51.755 5.792 −45.097 1.00 31.83 C ATOM 6628 O VAL D 48 52.849 6.093 −44.630 1.00 36.80 O ATOM 6629 CB VAL D 48 49.930 4.654 −43.824 1.00 30.07 C ATOM 6630 CG1 VAL D 48 51.056 3.761 −43.350 1.00 22.65 C ATOM 6631 CG2 VAL D 48 48.912 4.845 −42.723 1.00 27.78 C ATOM 6632 N ALA D 49 51.616 5.248 −46.300 1.00 35.77 N ATOM 6633 CA ALA D 49 52.777 5.006 −47.155 1.00 38.62 C ATOM 6634 C ALA D 49 53.495 6.310 −47.509 1.00 40.22 C ATOM 6635 O ALA D 49 54.725 6.359 −47.570 1.00 37.53 O ATOM 6636 CB ALA D 49 52.363 4.276 −48.411 1.00 30.17 C ATOM 6637 N GLY D 50 52.718 7.366 −47.728 1.00 39.60 N ATOM 6638 CA GLY D 50 53.263 8.651 −48.131 1.00 37.20 C ATOM 6639 C GLY D 50 53.988 9.403 −47.030 1.00 38.82 C ATOM 6640 O GLY D 50 54.955 10.109 −47.282 1.00 37.88 O ATOM 6641 N ASN D 51 53.519 9.264 −45.799 1.00 33.65 N ATOM 6642 CA ASN D 51 54.159 9.957 −44.694 1.00 31.72 C ATOM 6643 C ASN D 51 55.291 9.134 −44.130 1.00 31.26 C ATOM 6644 O ASN D 51 56.282 9.681 −43.685 1.00 36.48 O ATOM 6645 CB ASN D 51 53.145 10.330 −43.608 1.00 29.98 C ATOM 6646 CG ASN D 51 52.324 11.555 −43.983 1.00 37.23 C ATOM 6647 OD1 ASN D 51 52.764 12.697 −43.792 1.00 26.37 O ATOM 6648 ND2 ASN D 51 51.120 11.323 −44.527 1.00 29.89 N ATOM 6649 N VAL D 52 55.136 7.816 −44.147 1.00 30.02 N ATOM 6650 CA VAL D 52 56.237 6.929 −43.834 1.00 29.40 C ATOM 6651 C VAL D 52 57.365 7.238 −44.800 1.00 37.99 C ATOM 6652 O VAL D 52 58.538 7.177 −44.447 1.00 32.51 O ATOM 6653 CB VAL D 52 55.840 5.454 −43.986 1.00 36.39 C ATOM 6654 CG1 VAL D 52 57.076 4.585 −44.201 1.00 21.30 C ATOM 6655 CG2 VAL D 52 55.045 4.983 −42.760 1.00 33.79 C ATOM 6656 N LEU D 53 56.994 7.598 −46.023 1.00 44.61 N ATOM 6657 CA LEU D 53 57.968 7.879 −47.071 1.00 43.38 C ATOM 6658 C LEU D 53 58.694 9.214 −46.853 1.00 43.93 C ATOM 6659 O LEU D 53 59.896 9.311 −47.072 1.00 42.30 O ATOM 6660 CB LEU D 53 57.289 7.847 −48.437 1.00 38.10 C ATOM 6661 CG LEU D 53 58.097 7.179 −49.545 1.00 67.46 C ATOM 6662 CD1 LEU D 53 58.424 5.729 −49.189 1.00 53.95 C ATOM 6663 CD2 LEU D 53 57.335 7.255 −50.857 1.00 79.07 C ATOM 6664 N VAL D 54 57.957 10.234 −46.418 1.00 46.27 N ATOM 6665 CA VAL D 54 58.547 11.533 −46.107 1.00 37.90 C ATOM 6666 C VAL D 54 59.530 11.374 −44.959 1.00 40.66 C ATOM 6667 O VAL D 54 60.641 11.897 −44.985 1.00 40.02 O ATOM 6668 CB VAL D 54 57.472 12.571 −45.708 1.00 38.03 C ATOM 6669 CG1 VAL D 54 58.108 13.751 −44.994 1.00 37.10 C ATOM 6670 CG2 VAL D 54 56.678 13.043 −46.928 1.00 34.18 C ATOM 6671 N ILE D 55 59.109 10.636 −43.943 1.00 41.45 N ATOM 6672 CA ILE D 55 59.953 10.377 −42.788 1.00 44.15 C ATOM 6673 C ILE D 55 61.257 9.691 −43.207 1.00 51.35 C ATOM 6674 O ILE D 55 62.336 10.060 −42.745 1.00 60.92 O ATOM 6675 CB ILE D 55 59.192 9.553 −41.718 1.00 35.28 C ATOM 6676 CG1 ILE D 55 58.372 10.480 −40.820 1.00 29.86 C ATOM 6677 CG2 ILE D 55 60.136 8.731 −40.887 1.00 26.01 C ATOM 6678 CD1 ILE D 55 57.358 9.750 −39.981 1.00 33.25 C ATOM 6679 N ALA D 56 61.168 8.715 −44.101 1.00 49.27 N ATOM 6680 CA ALA D 56 62.352 7.968 −44.503 1.00 41.51 C ATOM 6681 C ALA D 56 63.265 8.805 −45.391 1.00 44.77 C ATOM 6682 O ALA D 56 64.479 8.723 −45.282 1.00 57.62 O ATOM 6683 CB ALA D 56 61.961 6.669 −45.199 1.00 41.32 C ATOM 6684 N ALA D 57 62.685 9.602 −46.276 1.00 40.32 N ATOM 6685 CA ALA D 57 63.481 10.455 −47.145 1.00 45.09 C ATOM 6686 C ALA D 57 64.287 11.448 −46.316 1.00 51.73 C ATOM 6687 O ALA D 57 65.493 11.592 −46.495 1.00 56.72 O ATOM 6688 CB ALA D 57 62.588 11.185 −48.156 1.00 38.80 C ATOM 6689 N ILE D 58 63.611 12.131 −45.402 1.00 51.31 N ATOM 6690 CA ILE D 58 64.264 13.101 −44.538 1.00 52.64 C ATOM 6691 C ILE D 58 65.345 12.422 −43.710 1.00 52.46 C ATOM 6692 O ILE D 58 66.323 13.051 −43.319 1.00 69.02 O ATOM 6693 CB ILE D 58 63.246 13.797 −43.603 1.00 50.59 C ATOM 6694 CG1 ILE D 58 62.404 14.810 −44.379 1.00 41.95 C ATOM 6695 CG2 ILE D 58 63.950 14.490 −42.448 1.00 50.05 C ATOM 6696 CD1 ILE D 58 61.272 15.405 −43.570 1.00 31.71 C ATOM 6697 N GLY D 59 65.166 11.131 −43.450 1.00 50.08 N ATOM 6698 CA GLY D 59 66.102 10.377 −42.634 1.00 56.47 C ATOM 6699 C GLY D 59 67.225 9.699 −43.410 1.00 58.41 C ATOM 6700 O GLY D 59 68.112 9.096 −42.820 1.00 59.21 O ATOM 6701 N SER D 60 67.185 9.781 −44.734 1.00 54.47 N ATOM 6702 CA SER D 60 68.256 9.240 −45.558 1.00 54.43 C ATOM 6703 C SER D 60 69.174 10.377 −45.954 1.00 67.14 C ATOM 6704 O SER D 60 70.239 10.557 −45.369 1.00 84.46 O ATOM 6705 CB SER D 60 67.700 8.573 −46.820 1.00 63.72 C ATOM 6706 OG SER D 60 67.110 7.319 −46.534 1.00 65.60 O ATOM 6707 N THR D 61 68.744 11.144 −46.953 1.00 69.90 N ATOM 6708 CA THR D 61 69.473 12.318 −47.422 1.00 70.17 C ATOM 6709 C THR D 61 69.738 13.299 −46.292 1.00 82.42 C ATOM 6710 O THR D 61 68.839 14.038 −45.891 1.00 83.13 O ATOM 6711 CB THR D 61 68.668 13.097 −48.471 1.00 63.98 C ATOM 6712 OG1 THR D 61 67.808 12.208 −49.193 1.00 69.96 O ATOM 6713 CG2 THR D 61 69.601 13.816 −49.433 1.00 80.94 C ATOM 6714 N GLN D 62 70.967 13.315 −45.786 1.00 92.10 N ATOM 6715 CA GLN D 62 71.358 14.298 −44.782 1.00 97.66 C ATOM 6716 C GLN D 62 71.250 15.687 −45.403 1.00 95.07 C ATOM 6717 O GLN D 62 71.073 16.693 −44.708 1.00 92.30 O ATOM 6718 CB GLN D 62 72.774 14.012 −44.289 1.00 106.21 C ATOM 6719 CG GLN D 62 72.878 12.691 −43.539 1.00 119.48 C ATOM 6720 CD GLN D 62 74.182 11.969 −43.796 1.00 137.39 C ATOM 6721 OE1 GLN D 62 75.220 12.594 −44.018 1.00 146.63 O ATOM 6722 NE2 GLN D 62 74.136 10.640 −43.768 1.00 135.26 N ATOM 6723 N ARG D 63 71.341 15.713 −46.729 1.00 74.98 N ATOM 6724 CA ARG D 63 71.112 16.909 −47.523 1.00 67.77 C ATOM 6725 C ARG D 63 69.652 17.379 −47.411 1.00 80.85 C ATOM 6726 O ARG D 63 69.312 18.502 −47.793 1.00 81.86 O ATOM 6727 CB ARG D 63 71.470 16.600 −48.976 1.00 89.41 C ATOM 6728 CG ARG D 63 70.981 17.608 −49.991 1.00 101.26 C ATOM 6729 CD ARG D 63 70.620 16.902 −51.278 1.00 102.07 C ATOM 6730 NE ARG D 63 70.776 17.762 −52.445 1.00 121.62 N ATOM 6731 CZ ARG D 63 70.251 17.496 −53.638 1.00 125.88 C ATOM 6732 NH1 ARG D 63 69.522 16.399 −53.811 1.00 117.63 N ATOM 6733 NH2 ARG D 63 70.445 18.327 −54.654 1.00 116.52 N ATOM 6734 N LEU D 64 68.791 16.502 −46.902 1.00 78.89 N ATOM 6735 CA LEU D 64 67.419 16.864 −46.561 1.00 67.09 C ATOM 6736 C LEU D 64 67.275 17.035 −45.048 1.00 66.22 C ATOM 6737 O LEU D 64 66.176 17.225 −44.538 1.00 55.43 O ATOM 6738 CB LEU D 64 66.436 15.795 −47.039 1.00 63.31 C ATOM 6739 CG LEU D 64 65.783 15.905 −48.419 1.00 59.21 C ATOM 6740 CD1 LEU D 64 64.736 14.808 −48.574 1.00 47.84 C ATOM 6741 CD2 LEU D 64 65.167 17.277 −48.659 1.00 43.21 C ATOM 6742 N GLN D 65 68.384 16.952 −44.326 1.00 73.42 N ATOM 6743 CA GLN D 65 68.340 17.148 −42.880 1.00 80.63 C ATOM 6744 C GLN D 65 68.621 18.597 −42.491 1.00 72.75 C ATOM 6745 O GLN D 65 69.768 19.042 −42.464 1.00 70.43 O ATOM 6746 CB GLN D 65 69.271 16.173 −42.158 1.00 79.32 C ATOM 6747 CG GLN D 65 68.582 14.868 −41.797 1.00 79.58 C ATOM 6748 CD GLN D 65 69.533 13.842 −41.225 1.00 98.69 C ATOM 6749 OE1 GLN D 65 70.667 13.709 −41.687 1.00 99.45 O ATOM 6750 NE2 GLN D 65 69.074 13.101 −40.217 1.00 94.97 N ATOM 6751 N THR D 66 67.545 19.326 −42.212 1.00 62.88 N ATOM 6752 CA THR D 66 67.609 20.740 −41.875 1.00 50.75 C ATOM 6753 C THR D 66 66.583 21.023 −40.783 1.00 45.40 C ATOM 6754 O THR D 66 65.666 20.234 −40.582 1.00 47.66 O ATOM 6755 CB THR D 66 67.321 21.626 −43.109 1.00 49.94 C ATOM 6756 OG1 THR D 66 65.960 21.466 −43.526 1.00 40.40 O ATOM 6757 CG2 THR D 66 68.228 21.240 −44.257 1.00 49.41 C ATOM 6758 N LEU D 67 66.750 22.129 −40.066 1.00 48.46 N ATOM 6759 CA LEU D 67 65.805 22.525 −39.027 1.00 44.51 C ATOM 6760 C LEU D 67 64.356 22.433 −39.493 1.00 47.00 C ATOM 6761 O LEU D 67 63.553 21.710 −38.903 1.00 44.65 O ATOM 6762 CB LEU D 67 66.085 23.956 −38.575 1.00 56.07 C ATOM 6763 CG LEU D 67 67.321 24.113 −37.706 1.00 51.03 C ATOM 6764 CD1 LEU D 67 67.290 25.460 −37.017 1.00 64.04 C ATOM 6765 CD2 LEU D 67 67.356 22.988 −36.698 1.00 48.12 C ATOM 6766 N THR D 68 64.026 23.183 −40.541 1.00 35.88 N ATOM 6767 CA THR D 68 62.681 23.170 −41.094 1.00 38.07 C ATOM 6768 C THR D 68 62.144 21.741 −41.282 1.00 39.06 C ATOM 6769 O THR D 68 60.975 21.470 −40.995 1.00 47.55 O ATOM 6770 CB THR D 68 62.595 23.968 −42.420 1.00 37.58 C ATOM 6771 OG1 THR D 68 62.813 25.362 −42.165 1.00 33.31 O ATOM 6772 CG2 THR D 68 61.231 23.803 −43.062 1.00 39.21 C ATOM 6773 N ASN D 69 62.996 20.823 −41.731 1.00 32.16 N ATOM 6774 CA ASN D 69 62.562 19.448 −42.004 1.00 35.45 C ATOM 6775 C ASN D 69 62.298 18.584 −40.773 1.00 32.38 C ATOM 6776 O ASN D 69 61.590 17.583 −40.852 1.00 29.77 O ATOM 6777 CB ASN D 69 63.523 18.748 −42.969 1.00 36.74 C ATOM 6778 CG ASN D 69 63.335 19.209 −44.401 1.00 51.61 C ATOM 6779 OD1 ASN D 69 62.291 19.763 −44.746 1.00 46.39 O ATOM 6780 ND2 ASN D 69 64.347 19.000 −45.237 1.00 58.25 N ATOM 6781 N LEU D 70 62.871 18.973 −39.641 1.00 35.10 N ATOM 6782 CA LEU D 70 62.557 18.339 −38.370 1.00 32.48 C ATOM 6783 C LEU D 70 61.097 18.621 −38.024 1.00 32.25 C ATOM 6784 O LEU D 70 60.359 17.730 −37.609 1.00 26.48 O ATOM 6785 CB LEU D 70 63.475 18.876 −37.272 1.00 41.98 C ATOM 6786 CG LEU D 70 64.810 18.172 −37.053 1.00 36.46 C ATOM 6787 CD1 LEU D 70 65.617 18.812 −35.904 1.00 28.53 C ATOM 6788 CD2 LEU D 70 64.520 16.712 −36.775 1.00 36.99 C ATOM 6789 N PHE D 71 60.685 19.868 −38.212 1.00 26.47 N ATOM 6790 CA PHE D 71 59.292 20.240 −38.023 1.00 34.44 C ATOM 6791 C PHE D 71 58.377 19.481 −38.985 1.00 37.54 C ATOM 6792 O PHE D 71 57.293 19.036 −38.601 1.00 33.37 O ATOM 6793 CB PHE D 71 59.114 21.746 −38.208 1.00 36.89 C ATOM 6794 CO PHE D 71 59.899 22.570 −37.231 1.00 38.76 C ATOM 6795 CD1 PHE D 71 60.115 22.115 −35.947 1.00 36.35 C ATOM 6796 CD2 PHE D 71 60.402 23.808 −37.590 1.00 41.40 C ATOM 6797 CE1 PHE D 71 60.829 22.874 −35.044 1.00 38.20 C ATOM 6798 CE2 PHE D 71 61.116 24.568 −36.688 1.00 37.54 C ATOM 6799 CZ PHE D 71 61.330 24.100 −35.417 1.00 30.84 C ATOM 6800 N ILE D 72 58.821 19.347 −40.233 1.00 31.96 N ATOM 6801 CA ILE D 72 58.094 18.587 −41.238 1.00 28.11 C ATOM 6802 C ILE D 72 57.831 17.160 −40.753 1.00 33.36 C ATOM 6803 O ILE D 72 56.767 16.580 −41.015 1.00 34.23 O ATOM 6804 CB ILE D 72 58.875 18.539 −42.568 1.00 33.79 C ATOM 6805 CG1 ILE D 72 58.883 19.916 −43.241 1.00 31.94 C ATOM 6806 CG2 ILE D 72 58.299 17.479 −43.508 1.00 33.20 C ATOM 6807 CD1 ILE D 72 57.529 20.511 −43.466 1.00 24.25 C ATOM 6808 N THR D 73 58.807 16.607 −40.039 1.00 30.89 N ATOM 6809 CA THR D 73 58.735 15.244 −39.519 1.00 33.76 C ATOM 6810 C THR D 73 57.726 15.123 −38.385 1.00 35.41 C ATOM 6811 O THR D 73 57.122 14.070 −38.182 1.00 37.41 O ATOM 6812 CB THR D 73 60.115 14.781 −38.995 1.00 26.78 C ATOM 6813 OG1 THR D 73 61.095 14.937 −40.027 1.00 22.82 O ATOM 6814 CG2 THR D 73 60.059 13.325 −38.551 1.00 16.71 C ATOM 6815 N SER D 74 57.580 16.201 −37.624 1.00 31.99 N ATOM 6816 CA SER D 74 56.601 16.244 −36.560 1.00 35.78 C ATOM 6817 C SER D 74 55.240 16.219 −37.247 1.00 36.44 C ATOM 6818 O SER D 74 54.337 15.466 −36.863 1.00 32.34 O ATOM 6819 CB SER D 74 56.782 17.527 −35.734 1.00 35.41 C ATOM 6820 OG SER D 74 55.823 17.636 −34.694 1.00 41.53 O ATOM 6821 N LEU D 75 55.133 17.040 −38.288 1.00 29.06 N ATOM 6822 CA LEU D 75 53.929 17.179 −39.083 1.00 23.55 C ATOM 6823 C LEU D 75 53.495 15.858 −39.702 1.00 28.81 C ATOM 6824 O LEU D 75 52.300 15.584 −39.820 1.00 31.50 O ATOM 6825 CB LEU D 75 54.169 18.203 −40.181 1.00 24.08 C ATOM 6826 CG LEU D 75 52.915 18.914 −40.667 1.00 26.85 C ATOM 6827 CD1 LEU D 75 51.889 18.976 −39.545 1.00 22.32 C ATOM 6828 CD2 LEU D 75 53.284 20.301 −41.177 1.00 22.76 C ATOM 6829 N ALA D 76 54.470 15.042 −40.092 1.00 25.99 N ATOM 6830 CA ALA D 76 54.209 13.740 −40.690 1.00 25.57 C ATOM 6831 C ALA D 76 53.797 12.662 −39.676 1.00 27.01 C ATOM 6832 O ALA D 76 53.124 11.694 −40.024 1.00 30.47 O ATOM 6833 CB ALA D 76 55.415 13.287 −41.486 1.00 22.65 C ATOM 6834 N CYS D 77 54.209 12.818 −38.425 1.00 28.50 N ATOM 6835 CA CYS D 77 53.779 11.893 −37.385 1.00 33.90 C ATOM 6836 C CYS D 77 52.332 12.162 −36.983 1.00 31.42 C ATOM 6837 O CYS D 77 51.557 11.228 −36.794 1.00 27.61 O ATOM 6838 CB CYS D 77 54.710 11.968 −36.181 1.00 31.40 C ATOM 6839 SG CYS D 77 56.357 11.314 −36.539 1.00 41.80 S ATOM 6840 N ALA D 78 51.974 13.439 −36.865 1.00 30.36 N ATOM 6841 CA ALA D 78 50.578 13.812 −36.695 1.00 30.55 C ATOM 6842 C ALA D 78 49.774 13.058 −37.741 1.00 31.48 C ATOM 6843 O ALA D 78 48.719 12.502 −37.448 1.00 28.66 O ATOM 6844 CB ALA D 78 50.392 15.308 −36.870 1.00 20.44 C ATOM 6845 N ASP D 79 50.311 13.023 −38.959 1.00 31.82 N ATOM 6846 CA ASP D 79 49.626 12.416 −40.095 1.00 26.35 C ATOM 6847 C ASP D 79 49.643 10.899 −40.052 1.00 25.56 C ATOM 6848 O ASP D 79 48.657 10.250 −40.380 1.00 25.49 O ATOM 6849 CB ASP D 79 50.201 12.930 −41.407 1.00 22.71 C ATOM 6850 CG ASP D 79 49.593 14.261 −41.826 1.00 34.62 C ATOM 6851 OD1 ASP D 79 48.789 14.828 −41.052 1.00 37.53 O ATOM 6852 OD2 ASP D 79 49.916 14.745 −42.934 1.00 54.22 O ATOM 6853 N LEU D 80 50.760 10.332 −39.622 1.00 31.51 N ATOM 6854 CA LEU D 80 50.832 8.896 −39.419 1.00 33.76 C ATOM 6855 C LEU D 80 49.759 8.431 −38.419 1.00 38.62 C ATOM 6856 O LEU D 80 49.118 7.390 −38.599 1.00 34.43 O ATOM 6857 CB LEU D 80 52.234 8.502 −38.948 1.00 38.39 C ATOM 6858 CG LEU D 80 52.699 7.136 −39.446 1.00 38.27 C ATOM 6859 CD1 LEU D 80 52.291 6.964 −40.891 1.00 36.50 C ATOM 6860 CD2 LEU D 80 54.199 6.997 −39.295 1.00 35.72 C ATOM 6861 N VAL D 81 49.550 9.206 −37.365 1.00 33.39 N ATOM 6862 CA VAL D 81 48.569 8.814 −36.369 1.00 37.23 C ATOM 6863 C VAL D 81 47.149 8.899 −36.936 1.00 32.14 C ATOM 6864 O VAL D 81 46.354 7.976 −36.770 1.00 37.01 O ATOM 6865 CB VAL D 81 48.741 9.610 −35.051 1.00 43.49 C ATOM 6866 CG1 VAL D 81 47.574 9.356 −34.089 1.00 24.72 C ATOM 6867 CG2 VAL D 81 50.070 9.234 −34.404 1.00 25.07 C ATOM 6868 N VAL D 82 46.839 9.994 −37.620 1.00 30.23 N ATOM 6869 CA VAL D 82 45.560 10.124 −38.320 1.00 35.59 C ATOM 6870 C VAL D 82 45.280 8.942 −39.255 1.00 33.53 C ATOM 6871 O VAL D 82 44.138 8.505 −39.401 1.00 29.91 O ATOM 6872 CB VAL D 82 45.518 11.406 −39.168 1.00 29.15 C ATOM 6873 CG1 VAL D 82 44.257 11.434 −40.031 1.00 25.07 C ATOM 6874 CG2 VAL D 82 45.615 12.631 −38.272 1.00 26.31 C ATOM 6875 N GLY D 83 46.334 8.431 −39.881 1.00 31.84 N ATOM 6876 CA GLY D 83 46.208 7.364 −40.853 1.00 37.73 C ATOM 6877 C GLY D 83 46.185 5.950 −40.304 1.00 32.19 C ATOM 6878 O GLY D 83 45.788 5.023 −40.996 1.00 37.70 O ATOM 6879 N LEU D 84 46.614 5.764 −39.067 1.00 35.57 N ATOM 6880 CA LEU D 84 46.685 4.416 −38.520 1.00 42.13 C ATOM 6881 C LEU D 84 45.612 4.149 −37.462 1.00 41.43 C ATOM 6882 O LEU D 84 45.114 3.029 −37.340 1.00 45.07 O ATOM 6883 CB LEU D 84 48.083 4.145 −37.955 1.00 39.34 C ATOM 6884 CG LEU D 84 49.187 4.014 −39.002 1.00 44.93 C ATOM 6885 CD1 LEU D 84 50.565 3.964 −38.354 1.00 33.60 C ATOM 6886 CD2 LEU D 84 48.940 2.776 −39.842 1.00 44.70 C ATOM 6887 N LEU D 85 45.253 5.177 −36.703 1.00 34.03 N ATOM 6888 CA LEU D 85 44.293 5.004 −35.624 1.00 39.34 C ATOM 6889 C LEU D 85 42.968 5.712 −35.889 1.00 36.37 C ATOM 6890 O LEU D 85 41.908 5.102 −35.791 1.00 46.03 O ATOM 6891 CB LEU D 85 44.910 5.459 −34.303 1.00 40.89 C ATOM 6892 CG LEU D 85 46.274 4.800 −34.081 1.00 41.00 C ATOM 6893 CD1 LEU D 85 46.977 5.398 −32.897 1.00 27.73 C ATOM 6894 CD2 LEU D 85 46.128 3.292 −33.914 1.00 36.09 C ATOM 6895 N VAL D 86 43.030 6.987 −36.253 1.00 32.34 N ATOM 6896 CA VAL D 86 41.825 7.789 −36.449 1.00 28.11 C ATOM 6897 C VAL D 86 40.971 7.325 −37.640 1.00 26.83 C ATOM 6898 O VAL D 86 39.848 6.861 −37.482 1.00 24.50 O ATOM 6899 CB VAL D 86 42.186 9.280 −36.632 1.00 22.85 C ATOM 6900 CG1 VAL D 86 40.940 10.108 −36.883 1.00 21.57 C ATOM 6901 CG2 VAL D 86 42.944 9.794 −35.436 1.00 19.43 C ATOM 6902 N VAL D 87 41.514 7.458 −38.842 1.00 37.84 N ATOM 6903 CA VAL D 87 40.756 7.163 −40.059 1.00 33.94 C ATOM 6904 C VAL D 87 40.257 5.711 −40.168 1.00 29.65 C ATOM 6905 O VAL D 87 39.112 5.480 −40.539 1.00 21.68 O ATOM 6906 CB VAL D 87 41.543 7.573 −41.324 1.00 29.08 C ATOM 6907 CG1 VAL D 87 41.107 6.750 −42.501 1.00 32.70 C ATOM 6908 CG2 VAL D 87 41.338 9.049 −41.612 1.00 33.35 C ATOM 6909 N PRO D 88 41.119 4.730 −39.851 1.00 31.52 N ATOM 6910 CA PRO D 88 40.611 3.362 −39.959 1.00 28.00 C ATOM 6911 C PRO D 88 39.378 3.118 −39.097 1.00 28.75 C ATOM 6912 O PRO D 88 38.404 2.562 −39.592 1.00 35.20 O ATOM 6913 CB PRO D 88 41.797 2.508 −39.512 1.00 24.80 C ATOM 6914 CG PRO D 88 42.978 3.320 −39.880 1.00 26.83 C ATOM 6915 CD PRO D 88 42.582 4.760 −39.670 1.00 31.53 C ATOM 6916 N PHE D 89 39.398 3.532 −37.838 1.00 35.40 N ATOM 6917 CA PHE D 89 38.225 3.329 −36.993 1.00 29.86 C ATOM 6918 C PHE D 89 37.039 4.189 −37.447 1.00 31.05 C ATOM 6919 O PHE D 89 35.896 3.731 −37.447 1.00 25.12 O ATOM 6920 CB PHE D 89 38.581 3.522 −35.521 1.00 25.15 C ATOM 6921 CG PHE D 89 39.414 2.406 −34.967 1.00 31.65 C ATOM 6922 CD1 PHE D 89 38.815 1.305 −34.377 1.00 28.63 C ATOM 6923 CD2 PHE D 89 40.798 2.435 −35.077 1.00 28.72 C ATOM 6924 CE1 PHE D 89 39.580 0.261 −33.875 1.00 31.49 C ATOM 6925 CE2 PHE D 89 41.573 1.397 −34.582 1.00 25.31 C ATOM 6926 CZ PHE D 89 40.961 0.307 −33.980 1.00 29.91 C ATOM 6927 N GLY D 90 37.323 5.418 −37.871 1.00 27.71 N ATOM 6928 CA GLY D 90 36.300 6.292 −38.410 1.00 28.44 C ATOM 6929 C GLY D 90 35.602 5.696 −39.626 1.00 42.35 C ATOM 6930 O GLY D 90 34.401 5.905 −39.838 1.00 36.51 O ATOM 6931 N ALA D 91 36.364 4.960 −40.432 1.00 38.65 N ATOM 6932 CA ALA D 91 35.817 4.243 −41.580 1.00 40.10 C ATOM 6933 C ALA D 91 34.797 3.162 −41.178 1.00 39.33 C ATOM 6934 O ALA D 91 33.736 3.057 −41.783 1.00 38.31 O ATOM 6935 CB ALA D 91 36.940 3.634 −42.411 1.00 26.37 C ATOM 6936 N THR D 92 35.119 2.359 −40.167 1.00 30.04 N ATOM 6937 CA THR D 92 34.186 1.339 −39.700 1.00 35.03 C ATOM 6938 C THR D 92 32.864 1.981 −39.275 1.00 41.42 C ATOM 6939 O THR D 92 31.791 1.446 −39.534 1.00 45.42 O ATOM 6940 CB THR D 92 34.761 0.492 −38.532 1.00 31.39 C ATOM 6941 OG1 THR D 92 35.047 1.337 −37.410 1.00 31.55 O ATOM 6942 CG2 THR D 92 36.039 −0.227 −38.957 1.00 35.33 C ATOM 6943 N LEU D 93 32.951 3.145 −38.642 1.00 37.78 N ATOM 6944 CA LEU D 93 31.775 3.843 −38.154 1.00 38.85 C ATOM 6945 C LEU D 93 30.891 4.369 −39.289 1.00 41.77 C ATOM 6946 O LEU D 93 29.707 4.041 −39.387 1.00 41.55 O ATOM 6947 CB LEU D 93 32.200 4.993 −37.240 1.00 41.11 C ATOM 6948 CG LEU D 93 31.094 5.876 −36.652 1.00 40.17 C ATOM 6949 CD1 LEU D 93 30.158 5.071 −35.753 1.00 32.64 C ATOM 6950 CD2 LEU D 93 31.721 7.020 −35.888 1.00 31.93 C ATOM 6951 N VAL D 94 31.462 5.201 −40.143 1.00 43.22 N ATOM 6952 CA VAL D 94 30.691 5.767 −41.242 1.00 53.36 C ATOM 6953 C VAL D 94 30.062 4.657 −42.087 1.00 49.22 C ATOM 6954 O VAL D 94 28.896 4.737 −42.462 1.00 48.15 O ATOM 6955 CB VAL D 94 31.543 6.706 −42.125 1.00 48.09 C ATOM 6956 CG1 VAL D 94 30.674 7.390 −43.140 1.00 45.33 C ATOM 6957 CG2 VAL D 94 32.244 7.753 −41.272 1.00 47.48 C ATOM 6958 N VAL D 95 30.828 3.615 −42.374 1.00 44.62 N ATOM 6959 CA VAL D 95 30.298 2.495 −43.145 1.00 53.38 C ATOM 6960 C VAL D 95 29.296 1.672 −42.344 1.00 52.07 C ATOM 6961 O VAL D 95 28.097 1.732 −42.599 1.00 56.06 O ATOM 6962 CB VAL D 95 31.419 1.582 −43.702 1.00 58.28 C ATOM 6963 CG1 VAL D 95 30.851 0.245 −44.167 1.00 57.40 C ATOM 6964 CG2 VAL D 95 32.142 2.275 −44.848 1.00 53.27 C ATOM 6965 N ARG D 96 29.800 0.916 −41.376 1.00 49.62 N ATOM 6966 CA ARG D 96 28.966 0.074 −40.529 1.00 56.75 C ATOM 6967 C ARG D 96 27.721 0.801 −39.977 1.00 54.46 C ATOM 6968 O ARG D 96 26.693 0.175 −39.702 1.00 52.19 O ATOM 6969 CB ARG D 96 29.815 −0.474 −39.387 1.00 52.90 C ATOM 6970 CG ARG D 96 29.068 −1.352 −38.426 1.00 80.81 C ATOM 6971 CD ARG D 96 28.655 −2.626 −39.111 1.00 96.40 C ATOM 6972 NE ARG D 96 27.368 −3.086 −38.611 1.00 104.56 N ATOM 6973 CZ ARG D 96 26.588 −3.933 −39.266 1.00 114.67 C ATOM 6974 NH1 ARG D 96 26.983 −4.411 −40.442 1.00 104.14 N ATOM 6975 NH2 ARG D 96 25.427 −4.308 −38.743 1.00 115.17 N ATOM 6976 N GLY D 97 27.825 2.120 −39.829 1.00 47.44 N ATOM 6977 CA GLY D 97 26.760 2.944 −39.281 1.00 35.72 C ATOM 6978 C GLY D 97 26.660 2.893 −37.760 1.00 46.17 C ATOM 6979 O GLY D 97 25.685 3.349 −37.180 1.00 37.40 O ATOM 6980 N THR D 98 27.670 2.335 −37.105 1.00 49.27 N ATOM 6981 CA THR D 98 27.623 2.158 −35.658 1.00 47.11 C ATOM 6982 C THR D 98 29.022 2.056 −35.079 1.00 44.03 C ATOM 6983 O THR D 98 29.947 1.632 −35.777 1.00 42.85 O ATOM 6984 CB THR D 98 26.797 0.911 −35.274 1.00 42.09 C ATOM 6985 OG1 THR D 98 25.495 1.324 −34.854 1.00 53.91 O ATOM 6986 CG2 THR D 98 27.448 0.155 −34.135 1.00 46.93 C ATOM 6987 N TRP D 99 29.179 2.464 −33.818 1.00 33.43 N ATOM 6988 CA TRP D 99 30.462 2.314 −33.140 1.00 33.99 C ATOM 6989 C TRP D 99 30.612 0.911 −32.586 1.00 29.88 C ATOM 6990 O TRP D 99 29.775 0.454 −31.820 1.00 38.52 O ATOM 6991 CB TRP D 99 30.665 3.343 −32.030 1.00 29.12 C ATOM 6992 CG TRP D 99 32.025 3.223 −31.464 1.00 30.04 C ATOM 6993 CD1 TRP D 99 32.380 2.612 −30.300 1.00 34.38 C ATOM 6994 CD2 TRP D 99 33.240 3.675 −32.067 1.00 37.82 C ATOM 6995 NE1 TRP D 99 33.738 2.682 −30.120 1.00 29.98 N ATOM 6996 CE2 TRP D 99 34.294 3.330 −31.194 1.00 41.85 C ATOM 6997 CE3 TRP D 99 33.543 4.349 −33.259 1.00 31.66 C ATOM 6998 CZ2 TRP D 99 35.633 3.635 −31.475 1.00 31.06 C ATOM 6999 CZ3 TRP D 99 34.872 4.661 −33.526 1.00 27.51 C ATOM 7000 CH2 TRP D 99 35.895 4.300 −32.639 1.00 22.61 C ATOM 7001 N LEU D 100 31.696 0.242 −32.966 1.00 32.61 N ATOM 7002 CA LEU D 100 31.850 −1.190 −32.730 1.00 31.51 C ATOM 7003 C LEU D 100 32.892 −1.516 −31.676 1.00 31.85 C ATOM 7004 O LEU D 100 33.167 −2.687 −31.403 1.00 35.77 O ATOM 7005 CB LEU D 100 32.244 −1.897 −34.036 1.00 36.48 C ATOM 7006 CG LEU D 100 31.221 −1.918 −35.174 1.00 47.33 C ATOM 7007 CD1 LEU D 100 31.820 −2.526 −36.429 1.00 41.55 C ATOM 7008 CD2 LEU D 100 29.980 −2.680 −34.750 1.00 29.84 C ATOM 7009 N TRP D 101 33.482 −0.494 −31.081 1.00 26.11 N ATOM 7010 CA TRP D 101 34.654 −0.742 −30.263 1.00 33.17 C ATOM 7011 C TRP D 101 34.505 −0.484 −28.752 1.00 31.78 C ATOM 7012 O TRP D 101 35.458 −0.642 −28.001 1.00 35.01 O ATOM 7013 CB TRP D 101 35.837 0.023 −30.860 1.00 34.73 C ATOM 7014 CG TRP D 101 35.982 −0.256 −32.319 1.00 23.39 C ATOM 7015 CD1 TRP D 101 35.435 0.451 −33.344 1.00 32.33 C ATOM 7016 CD2 TRP D 101 36.705 −1.330 −32.914 1.00 25.24 C ATOM 7017 NE1 TRP D 101 35.778 −0.112 −34.554 1.00 27.57 N ATOM 7018 CE2 TRP D 101 36.556 −1.208 −34.317 1.00 26.96 C ATOM 7019 CE3 TRP D 101 37.478 −2.374 −32.407 1.00 26.35 C ATOM 7020 CZ2 TRP D 101 37.143 −2.092 −35.208 1.00 27.47 C ATOM 7021 CZ3 TRP D 101 38.064 −3.253 −33.293 1.00 32.72 C ATOM 7022 CH2 TRP D 101 37.892 −3.110 −34.679 1.00 38.55 C ATOM 7023 N GLY D 102 33.315 −0.104 −28.306 1.00 39.06 N ATOM 7024 CA GLY D 102 33.109 0.163 −26.894 1.00 44.18 C ATOM 7025 C GLY D 102 33.325 1.626 −26.568 1.00 44.57 C ATOM 7026 O GLY D 102 34.031 2.323 −27.295 1.00 44.14 O ATOM 7027 N SER D 103 32.730 2.092 −25.471 1.00 53.52 N ATOM 7028 CA SER D 103 32.701 3.527 −25.175 1.00 50.60 C ATOM 7029 C SER D 103 34.065 4.142 −24.844 1.00 37.48 C ATOM 7030 O SER D 103 34.329 5.282 −25.215 1.00 44.41 O ATOM 7031 CB SER D 103 31.671 3.847 −24.091 1.00 36.24 C ATOM 7032 OG SER D 103 31.813 2.978 −22.990 1.00 47.97 O ATOM 7033 N PHE D 104 34.932 3.397 −24.167 1.00 32.98 N ATOM 7034 CA PHE D 104 36.278 3.896 −23.895 1.00 39.66 C ATOM 7035 C PHE D 104 37.129 4.162 −25.148 1.00 37.87 C ATOM 7036 O PHE D 104 37.765 5.209 −25.271 1.00 26.43 O ATOM 7037 CB PHE D 104 37.060 2.953 −22.991 1.00 32.70 C ATOM 7038 CG PHE D 104 38.482 3.367 −22.825 1.00 34.01 C ATOM 7039 CD1 PHE D 104 38.826 4.359 −21.913 1.00 35.26 C ATOM 7040 CD2 PHE D 104 39.473 2.817 −23.624 1.00 39.77 C ATOM 7041 CE1 PHE D 104 40.143 4.768 −21.774 1.00 41.98 C ATOM 7042 CE2 PHE D 104 40.796 3.214 −23.487 1.00 39.06 C ATOM 7043 CZ PHE D 104 41.132 4.192 −22.564 1.00 36.64 C ATOM 7044 N LEU D 105 37.167 3.191 −26.052 1.00 31.65 N ATOM 7045 CA LEU D 105 37.885 3.366 −27.302 1.00 34.85 C ATOM 7046 C LEU D 105 37.282 4.512 −28.122 1.00 33.62 C ATOM 7047 O LEU D 105 37.993 5.218 −28.844 1.00 21.47 O ATOM 7048 CB LEU D 105 37.927 2.058 −28.097 1.00 31.29 C ATOM 7049 CG LEU D 105 39.003 1.096 −27.583 1.00 32.71 C ATOM 7050 CD1 LEU D 105 39.010 −0.219 −28.373 1.00 23.98 C ATOM 7051 CD2 LEU D 105 40.369 1.779 −27.621 1.00 26.77 C ATOM 7052 N CYS D 106 35.974 4.712 −27.985 1.00 28.78 N ATOM 7053 CA CYS D 106 35.326 5.854 −28.607 1.00 25.43 C ATOM 7054 C CYS D 106 35.891 7.159 −28.055 1.00 29.61 C ATOM 7055 O CYS D 106 36.194 8.090 −28.806 1.00 25.98 O ATOM 7056 CB CYS D 106 33.814 5.805 −28.408 1.00 31.59 C ATOM 7057 SG CYS D 106 32.967 7.370 −28.767 1.00 35.64 S ATOM 7058 N GLU D 107 36.047 7.233 −26.741 1.00 27.17 N ATOM 7059 CA GLU D 107 36.561 8.458 −26.147 1.00 25.63 C ATOM 7060 C GLU D 107 38.070 8.630 −26.350 1.00 25.32 C ATOM 7061 O GLU D 107 38.552 9.750 −26.520 1.00 22.17 O ATOM 7062 CB GLU D 107 36.159 8.559 −24.681 1.00 30.41 C ATOM 7063 CG GLU D 107 34.670 8.745 −24.504 1.00 25.62 C ATOM 7064 CD GLU D 107 34.210 8.501 −23.083 1.00 37.52 C ATOM 7065 OE1 GLU D 107 34.938 8.879 −22.137 1.00 45.13 O ATOM 7066 OE2 GLU D 107 33.110 7.936 −22.913 1.00 50.79 O ATOM 7067 N LEU D 108 38.810 7.527 −26.362 1.00 20.38 N ATOM 7068 CA LEU D 108 40.228 7.584 −26.717 1.00 27.40 C ATOM 7069 C LEU D 108 40.449 8.014 −28.178 1.00 32.97 C ATOM 7070 O LEU D 108 41.340 8.813 −28.478 1.00 25.92 O ATOM 7071 CB LEU D 108 40.908 6.244 −26.462 1.00 25.29 C ATOM 7072 CG LEU D 108 42.382 6.240 −26.859 1.00 23.27 C ATOM 7073 CD1 LEU D 108 43.104 7.426 −26.225 1.00 23.41 C ATOM 7074 CD2 LEU D 108 43.051 4.919 −26.488 1.00 20.13 C ATOM 7075 N TRP D 109 39.616 7.470 −29.064 1.00 30.02 N ATOM 7076 CA TRP D 109 39.598 7.781 −30.489 1.00 20.96 C ATOM 7077 C TRP D 109 39.370 9.259 −30.766 1.00 26.35 C ATOM 7078 O TRP D 109 40.109 9.884 −31.533 1.00 29.28 O ATOM 7079 CB TRP D 109 38.481 6.974 −31.163 1.00 21.29 C ATOM 7080 CG TRP D 109 38.306 7.272 −32.626 1.00 27.20 C ATOM 7081 CD1 TRP D 109 39.224 7.063 −33.619 1.00 21.75 C ATOM 7082 CD2 TRP D 109 37.139 7.807 −33.268 1.00 28.71 C ATOM 7083 NE1 TRP D 109 38.715 7.455 −34.824 1.00 22.69 N ATOM 7084 CE2 TRP D 109 37.437 7.912 −34.646 1.00 26.89 C ATOM 7085 CE3 TRP D 109 35.880 8.213 −32.818 1.00 24.04 C ATOM 7086 CZ2 TRP D 109 36.517 8.407 −35.580 1.00 29.22 C ATOM 7087 CZ3 TRP D 109 34.967 8.715 −33.744 1.00 28.02 C ATOM 7088 CH2 TRP D 109 35.288 8.797 −35.111 1.00 29.74 C ATOM 7089 N THR D 110 38.323 9.800 −30.157 1.00 20.99 N ATOM 7090 CA THR D 110 37.973 11.204 −30.288 1.00 24.59 C ATOM 7091 C THR D 110 39.140 12.072 −29.841 1.00 29.06 C ATOM 7092 O THR D 110 39.415 13.128 −30.416 1.00 18.84 O ATOM 7093 CB THR D 110 36.748 11.524 −29.400 1.00 28.97 C ATOM 7094 OG1 THR D 110 35.633 10.746 −29.845 1.00 22.96 O ATOM 7095 CG2 THR D 110 36.394 13.026 −29.417 1.00 15.16 C ATOM 7096 N SER D 111 39.810 11.603 −28.793 1.00 33.82 N ATOM 7097 CA SER D 111 40.989 12.255 −28.239 1.00 30.23 C ATOM 7098 C SER D 111 42.120 12.395 −29.257 1.00 32.09 C ATOM 7099 O SER D 111 42.658 13.486 −29.444 1.00 28.55 O ATOM 7100 CB SER D 111 41.491 11.461 −27.037 1.00 25.25 C ATOM 7101 OG SER D 111 40.771 11.812 −25.879 1.00 44.62 O ATOM 7102 N LEU D 112 42.490 11.279 −29.885 1.00 26.57 N ATOM 7103 CA LEU D 112 43.571 11.254 −30.862 1.00 25.30 C ATOM 7104 C LEU D 112 43.193 12.118 −32.063 1.00 24.23 C ATOM 7105 O LEU D 112 44.015 12.840 −32.633 1.00 17.98 O ATOM 7106 CB LEU D 112 43.861 9.812 −31.284 1.00 17.98 C ATOM 7107 CG LEU D 112 44.276 8.912 −30.107 1.00 25.37 C ATOM 7108 CD1 LEU D 112 44.333 7.433 −30.477 1.00 17.63 C ATOM 7109 CD2 LEU D 112 45.602 9.359 −29.529 1.00 16.55 C ATOM 7110 N ASP D 113 41.925 12.059 −32.428 1.00 18.65 N ATOM 7111 CA ASP D 113 41.441 12.866 −33.525 1.00 20.04 C ATOM 7112 C ASP D 113 41.628 14.361 −33.218 1.00 27.56 C ATOM 7113 O ASP D 113 42.108 15.120 −34.062 1.00 28.79 O ATOM 7114 CB ASP D 113 39.990 12.518 −33.791 1.00 21.17 C ATOM 7115 CG ASP D 113 39.465 13.123 −35.065 1.00 24.14 C ATOM 7116 OD1 ASP D 113 40.010 14.131 −35.538 1.00 24.70 O ATOM 7117 OD2 ASP D 113 38.484 12.580 −35.593 1.00 32.67 O ATOM 7118 N VAL D 114 41.270 14.772 −32.003 1.00 25.29 N ATOM 7119 CA VAL D 114 41.441 16.153 −31.558 1.00 21.34 C ATOM 7120 C VAL D 114 42.913 16.565 −31.424 1.00 22.52 C ATOM 7121 O VAL D 114 43.302 17.657 −31.846 1.00 22.49 O ATOM 7122 CB VAL D 114 40.713 16.393 −30.227 1.00 19.96 C ATOM 7123 CG1 VAL D 114 40.865 17.838 −29.777 1.00 19.99 C ATOM 7124 CG2 VAL D 114 39.257 16.057 −30.378 1.00 25.51 C ATOM 7125 N LEU D 115 43.717 15.688 −30.834 1.00 20.14 N ATOM 7126 CA LEU D 115 45.164 15.868 −30.718 1.00 18.57 C ATOM 7127 C LEU D 115 45.832 16.238 −32.034 1.00 28.13 C ATOM 7128 O LEU D 115 46.560 17.233 −32.130 1.00 25.02 O ATOM 7129 CB LEU D 115 45.797 14.576 −30.216 1.00 19.00 C ATOM 7130 CG LEU D 115 47.293 14.613 −29.925 1.00 27.87 C ATOM 7131 CD1 LEU D 115 47.597 15.596 −28.818 1.00 19.58 C ATOM 7132 CD2 LEU D 115 47.791 13.221 −29.574 1.00 23.65 C ATOM 7133 N CYS D 116 45.569 15.425 −33.050 1.00 30.76 N ATOM 7134 CA CYS D 116 46.291 15.506 −34.312 1.00 23.94 C ATOM 7135 C CYS D 116 46.042 16.809 −35.065 1.00 24.41 C ATOM 7136 O CYS D 116 46.985 17.419 −35.570 1.00 23.74 O ATOM 7137 CB CYS D 116 45.968 14.286 −35.176 1.00 26.28 C ATOM 7138 SG CYS D 116 46.752 12.770 −34.572 1.00 38.72 S ATOM 7139 N VAL D 117 44.782 17.234 −35.135 1.00 19.43 N ATOM 7140 CA VAL D 117 44.449 18.528 −35.729 1.00 19.67 C ATOM 7141 C VAL D 117 45.139 19.652 −34.958 1.00 22.39 C ATOM 7142 O VAL D 117 45.689 20.576 −35.546 1.00 17.92 O ATOM 7143 CB VAL D 117 42.927 18.790 −35.714 1.00 19.31 C ATOM 7144 CG1 VAL D 117 42.606 20.109 −36.390 1.00 18.44 C ATOM 7145 CG2 VAL D 117 42.194 17.665 −36.378 1.00 20.44 C ATOM 7146 N THR D 118 45.106 19.563 −33.632 1.00 26.49 N ATOM 7147 CA THR D 118 45.722 20.575 −32.778 1.00 23.05 C ATOM 7148 C THR D 118 47.244 20.630 −32.934 1.00 21.98 C ATOM 7149 O THR D 118 47.825 21.704 −33.113 1.00 22.16 O ATOM 7150 CB THR D 118 45.360 20.333 −31.319 1.00 22.88 C ATOM 7151 OG1 THR D 118 43.933 20.317 −31.188 1.00 33.77 O ATOM 7152 CG2 THR D 118 45.931 21.425 −30.432 1.00 23.57 C ATOM 7153 N ALA D 119 47.892 19.476 −32.881 1.00 12.26 N ATOM 7154 CA ALA D 119 49.331 19.443 −33.069 1.00 17.27 C ATOM 7155 C ALA D 119 49.772 19.946 −34.479 1.00 26.22 C ATOM 7156 O ALA D 119 50.793 20.613 −34.618 1.00 25.05 O ATOM 7157 CB ALA D 119 49.867 18.043 −32.795 1.00 15.38 C ATOM 7158 N SER D 120 49.004 19.618 −35.513 1.00 18.91 N ATOM 7159 CA SER D 120 49.355 19.982 −36.872 1.00 20.60 C ATOM 7160 C SER D 120 49.422 21.489 −37.018 1.00 24.27 C ATOM 7161 O SER D 120 50.432 22.041 −37.471 1.00 24.52 O ATOM 7162 CB SER D 120 48.335 19.418 −37.873 1.00 17.31 C ATOM 7163 OG SER D 120 48.401 18.009 −37.927 1.00 25.97 O ATOM 7164 N ILE D 121 48.334 22.146 −36.637 1.00 22.68 N ATOM 7165 CA ILE D 121 48.193 23.580 −36.824 1.00 22.41 C ATOM 7166 C ILE D 121 49.158 24.335 −35.908 1.00 21.99 C ATOM 7167 O ILE D 121 49.636 25.412 −36.247 1.00 30.29 O ATOM 7168 CB ILE D 121 46.742 24.026 −36.596 1.00 21.99 C ATOM 7169 CG1 ILE D 121 46.613 25.544 −36.720 1.00 23.48 C ATOM 7170 CG2 ILE D 121 46.270 23.562 −35.231 1.00 27.54 C ATOM 7171 CD1 ILE D 121 47.181 26.100 −37.992 1.00 21.52 C ATOM 7172 N GLU D 122 49.472 23.768 −34.757 1.00 19.88 N ATOM 7173 CA GLU D 122 50.502 24.374 −33.931 1.00 24.82 C ATOM 7174 C GLU D 122 51.874 24.246 −34.610 1.00 27.23 C ATOM 7175 O GLU D 122 52.605 25.229 −34.742 1.00 27.06 O ATOM 7176 CB GLU D 122 50.490 23.788 −32.510 1.00 24.98 C ATOM 7177 CG GLU D 122 49.316 24.301 −31.667 1.00 41.10 C ATOM 7178 CD GLU D 122 49.343 23.843 −30.205 1.00 51.07 C ATOM 7179 OE1 GLU D 122 50.446 23.723 −29.627 1.00 53.01 O ATOM 7180 OE2 GLU D 122 48.250 23.620 −29.629 1.00 44.17 O ATOM 7181 N THR D 123 52.208 23.040 −35.060 1.00 21.46 N ATOM 7182 CA THR D 123 53.458 22.810 −35.764 1.00 18.37 C ATOM 7183 C THR D 123 53.606 23.733 −36.978 1.00 27.70 C ATOM 7184 O THR D 123 54.707 24.187 −37.274 1.00 25.89 O ATOM 7185 CB THR D 123 53.606 21.333 −36.189 1.00 24.89 C ATOM 7186 OG1 THR D 123 53.621 20.496 −35.025 1.00 30.98 O ATOM 7187 CG2 THR D 123 54.893 21.118 −36.963 1.00 24.29 C ATOM 7188 N LEU D 124 52.502 24.017 −37.672 1.00 26.04 N ATOM 7189 CA LEU D 124 52.532 24.933 −38.811 1.00 22.00 C ATOM 7190 C LEU D 124 52.848 26.360 −38.383 1.00 26.62 C ATOM 7191 O LEU D 124 53.539 27.087 −39.087 1.00 22.50 O ATOM 7192 CB LEU D 124 51.211 24.903 −39.579 1.00 24.01 C ATOM 7193 CG LEU D 124 50.949 23.692 −40.490 1.00 28.23 C ATOM 7194 CD1 LEU D 124 49.615 23.817 −41.194 1.00 25.35 C ATOM 7195 CD2 LEU D 124 52.055 23.506 −41.504 1.00 19.24 C ATOM 7196 N CYS D 125 52.327 26.758 −37.228 1.00 29.70 N ATOM 7197 CA CYS D 125 52.687 28.038 −36.616 1.00 31.36 C ATOM 7198 C CYS D 125 54.181 28.163 −36.387 1.00 31.44 C ATOM 7199 O CYS D 125 54.802 29.149 −36.779 1.00 29.80 O ATOM 7200 CB CYS D 125 52.003 28.188 −35.268 1.00 28.98 C ATOM 7201 SG CYS D 125 50.426 28.943 −35.374 1.00 48.66 S ATOM 7202 N VAL D 126 54.742 27.162 −35.715 1.00 28.48 N ATOM 7203 CA VAL D 126 56.166 27.131 −35.421 1.00 29.41 C ATOM 7204 C VAL D 126 56.971 27.248 −36.706 1.00 28.75 C ATOM 7205 O VAL D 126 57.924 28.005 −36.770 1.00 32.07 O ATOM 7206 CB VAL D 126 56.560 25.844 −34.669 1.00 33.33 C ATOM 7207 CG1 VAL D 126 58.065 25.679 −34.631 1.00 26.39 C ATOM 7208 CG2 VAL D 126 55.971 25.844 −33.262 1.00 25.43 C ATOM 7209 N ILE D 127 56.576 26.503 −37.732 1.00 31.64 N ATOM 7210 CA ILE D 127 57.242 26.573 −39.029 1.00 32.65 C ATOM 7211 C ILE D 127 57.240 28.001 −39.632 1.00 33.20 C ATOM 7212 O ILE D 127 58.263 28.472 −40.135 1.00 30.59 O ATOM 7213 CB ILE D 127 56.656 25.551 −40.019 1.00 27.28 C ATOM 7214 CG1 ILE D 127 57.021 24.132 −39.587 1.00 19.26 C ATOM 7215 CG2 ILE D 127 57.170 25.823 −41.426 1.00 25.83 C ATOM 7216 CD1 ILE D 127 56.201 23.073 −40.249 1.00 20.29 C ATOM 7217 N ALA D 128 56.107 28.691 −39.569 1.00 25.46 N ATOM 7218 CA ALA D 128 56.051 30.083 −40.011 1.00 30.35 C ATOM 7219 C ALA D 128 56.998 30.984 −39.209 1.00 40.13 C ATOM 7220 O ALA D 128 57.772 31.746 −39.784 1.00 41.89 O ATOM 7221 CB ALA D 128 54.624 30.620 −39.930 1.00 28.08 C ATOM 7222 N ILE D 129 56.919 30.897 −37.882 1.00 29.49 N ATOM 7223 CA ILE D 129 57.730 31.724 −37.000 1.00 30.99 C ATOM 7224 C ILE D 129 59.232 31.468 −37.186 1.00 37.64 C ATOM 7225 O ILE D 129 60.040 32.399 −37.158 1.00 34.75 O ATOM 7226 CB ILE D 129 57.298 31.526 −35.515 1.00 30.59 C ATOM 7227 CG1 ILE D 129 55.998 32.279 −35.242 1.00 27.46 C ATOM 7228 CG2 ILE D 129 58.375 31.982 −34.533 1.00 18.38 C ATOM 7229 CD1 ILE D 129 55.286 31.802 −34.019 1.00 18.07 C ATOM 7230 N ASP D 130 59.584 30.201 −37.384 1.00 36.33 N ATOM 7231 CA ASP D 130 60.962 29.762 −37.568 1.00 30.99 C ATOM 7232 C ASP D 130 61.544 30.376 −38.836 1.00 37.76 C ATOM 7233 O ASP D 130 62.634 30.949 −38.811 1.00 42.14 O ATOM 7234 CB ASP D 130 60.998 28.222 −37.621 1.00 45.95 C ATOM 7235 CG ASP D 130 62.320 27.658 −38.149 1.00 56.11 C ATOM 7236 OD1 ASP D 130 63.341 27.696 −37.415 1.00 55.76 O ATOM 7237 OD2 ASP D 130 62.319 27.134 −39.286 1.00 41.10 O ATOM 7238 N ARG D 131 60.801 30.269 −39.936 1.00 38.66 N ATOM 7239 CA ARG D 131 61.207 30.863 −41.214 1.00 42.45 C ATOM 7240 C ARG D 131 61.283 32.389 −41.153 1.00 32.35 C ATOM 7241 O ARG D 131 62.277 32.981 −41.544 1.00 46.98 O ATOM 7242 CB ARG D 131 60.282 30.417 −42.360 1.00 32.61 C ATOM 7243 CG ARG D 131 60.496 28.969 −42.830 1.00 36.10 C ATOM 7244 CD ARG D 131 61.934 28.701 −43.255 1.00 39.49 C ATOM 7245 NE ARG D 131 62.809 28.409 −42.122 1.00 45.27 N ATOM 7246 CZ ARG D 131 64.139 28.452 −42.171 1.00 50.57 C ATOM 7247 NH1 ARG D 131 64.754 28.782 −43.297 1.00 59.19 N ATOM 7248 NH2 ARG D 131 64.862 28.168 −41.096 1.00 52.30 N ATOM 7249 N TYR D 132 60.233 33.027 −40.668 1.00 28.95 N ATOM 7250 CA TYR D 132 60.274 34.468 −40.440 1.00 42.35 C ATOM 7251 C TYR D 132 61.523 34.937 −39.667 1.00 50.77 C ATOM 7252 O TYR D 132 62.113 35.970 −39.995 1.00 45.24 O ATOM 7253 CB TYR D 132 59.024 34.926 −39.692 1.00 39.60 C ATOM 7254 CG TYR D 132 59.106 36.367 −39.278 1.00 52.78 C ATOM 7255 CD1 TYR D 132 58.761 37.384 −40.167 1.00 52.73 C ATOM 7256 CD2 TYR D 132 59.557 36.721 −38.010 1.00 51.67 C ATOM 7257 CE1 TYR D 132 58.844 38.713 −39.799 1.00 48.83 C ATOM 7258 CE2 TYR D 132 59.643 38.051 −37.631 1.00 54.01 C ATOM 7259 CZ TYR D 132 59.284 39.039 −38.531 1.00 57.96 C ATOM 7260 OH TYR D 132 59.368 40.359 −38.163 1.00 73.34 O ATOM 7261 N LEU D 133 61.904 34.193 −38.629 1.00 40.20 N ATOM 7262 CA LEU D 133 63.051 34.564 −37.818 1.00 42.77 C ATOM 7263 C LEU D 133 64.364 34.239 −38.513 1.00 54.19 C ATOM 7264 O LEU D 133 65.353 34.947 −38.340 1.00 61.64 O ATOM 7265 CB LEU D 133 62.993 33.909 −36.431 1.00 43.88 C ATOM 7266 CG LEU D 133 61.910 34.453 −35.482 1.00 49.77 C ATOM 7267 CD1 LEU D 133 61.963 33.745 −34.150 1.00 25.18 C ATOM 7268 CD2 LEU D 133 62.000 35.970 −35.279 1.00 40.95 C ATOM 7269 N ALA D 134 64.378 33.173 −39.304 1.00 46.77 N ATOM 7270 CA ALA D 134 65.580 32.817 −40.044 1.00 44.43 C ATOM 7271 C ALA D 134 65.869 33.844 −41.139 1.00 54.38 C ATOM 7272 O ALA D 134 66.939 33.834 −41.748 1.00 59.62 O ATOM 7273 CB ALA D 134 65.445 31.429 −40.639 1.00 34.46 C ATOM 7274 N ILE D 135 64.923 34.750 −41.365 1.00 54.30 N ATOM 7275 CA ILE D 135 64.951 35.592 −42.558 1.00 60.70 C ATOM 7276 C ILE D 135 65.088 37.084 −42.260 1.00 52.86 C ATOM 7277 O ILE D 135 65.063 37.905 −43.168 1.00 61.82 O ATOM 7278 CB ILE D 135 63.675 35.375 −43.405 1.00 52.94 C ATOM 7279 CG1 ILE D 135 64.021 35.201 −44.875 1.00 46.16 C ATOM 7280 CG2 ILE D 135 62.691 36.519 −43.215 1.00 52.57 C ATOM 7281 CD1 ILE D 135 62.792 35.103 −45.752 1.00 62.45 C ATOM 7282 N THR D 136 65.229 37.436 −40.992 1.00 56.84 N ATOM 7283 CA THR D 136 65.285 38.840 −40.609 1.00 60.28 C ATOM 7284 C THR D 136 66.332 39.052 −39.522 1.00 65.78 C ATOM 7285 O THR D 136 66.704 40.183 −39.203 1.00 71.16 O ATOM 7286 CB THR D 136 63.902 39.353 −40.118 1.00 60.24 C ATOM 7287 OG1 THR D 136 63.447 38.565 −39.008 1.00 57.76 O ATOM 7288 CG2 THR D 136 62.877 39.270 −41.227 1.00 55.60 C ATOM 7289 N SER D 137 66.803 37.947 −38.959 1.00 56.23 N ATOM 7290 CA SER D 137 67.750 37.980 −37.859 1.00 60.26 C ATOM 7291 C SER D 137 68.614 36.738 −37.969 1.00 52.35 C ATOM 7292 O SER D 137 68.758 35.990 −37.000 1.00 53.84 O ATOM 7293 CB SER D 137 66.998 37.976 −36.525 1.00 61.61 C ATOM 7294 OG SER D 137 65.749 38.646 −36.643 1.00 53.92 O ATOM 7295 N PRO D 138 69.199 36.519 −39.157 1.00 51.90 N ATOM 7296 CA PRO D 138 69.876 35.264 −39.520 1.00 58.52 C ATOM 7297 C PRO D 138 71.044 34.922 −38.592 1.00 59.59 C ATOM 7298 O PRO D 138 71.342 33.741 −38.388 1.00 50.53 O ATOM 7299 CB PRO D 138 70.397 35.528 −40.945 1.00 42.86 C ATOM 7300 CG PRO D 138 69.698 36.753 −41.409 1.00 44.87 C ATOM 7301 CD PRO D 138 69.396 37.556 −40.180 1.00 55.81 C ATOM 7302 N PHE D 139 71.704 35.938 −38.043 1.00 57.77 N ATOM 7303 CA PHE D 139 72.817 35.670 −37.153 1.00 61.18 C ATOM 7304 C PHE D 139 72.277 35.055 −35.888 1.00 56.87 C ATOM 7305 O PHE D 139 72.607 33.915 −35.543 1.00 51.09 O ATOM 7306 CB PHE D 139 73.596 36.938 −36.807 1.00 64.99 C ATOM 7307 CG PHE D 139 74.750 36.689 −35.880 1.00 63.77 C ATOM 7308 CD1 PHE D 139 75.910 36.093 −36.351 1.00 58.48 C ATOM 7309 CD2 PHE D 139 74.665 37.022 −34.533 1.00 68.97 C ATOM 7310 CE1 PHE D 139 76.972 35.848 −35.506 1.00 65.26 C ATOM 7311 CE2 PHE D 139 75.723 36.783 −33.678 1.00 64.08 C ATOM 7312 CZ PHE D 139 76.881 36.195 −34.166 1.00 72.74 C ATOM 7313 N ARG D 140 71.442 35.830 −35.202 1.00 62.03 N ATOM 7314 CA ARG D 140 70.795 35.372 −33.980 1.00 71.43 C ATOM 7315 C ARG D 140 70.083 34.047 −34.229 1.00 56.54 C ATOM 7316 O ARG D 140 69.984 33.204 −33.334 1.00 51.99 O ATOM 7317 CB ARG D 140 69.821 36.427 −33.449 1.00 68.76 C ATOM 7318 CG ARG D 140 70.499 37.634 −32.805 1.00 74.38 C ATOM 7319 CD ARG D 140 69.479 38.590 −32.205 1.00 94.48 C ATOM 7320 NE ARG D 140 70.050 39.380 −31.116 1.00 116.70 N ATOM 7321 CZ ARG D 140 69.338 40.148 −30.295 1.00 131.79 C ATOM 7322 NH1 ARG D 140 68.021 40.232 −30.439 1.00 125.97 N ATOM 7323 NH2 ARG D 140 69.943 40.830 −29.329 1.00 132.49 N ATOM 7324 N TYR D 141 69.608 33.856 −35.453 1.00 42.68 N ATOM 7325 CA TYR D 141 68.998 32.590 −35.803 1.00 41.47 C ATOM 7326 C TYR D 141 70.015 31.449 −35.852 1.00 50.99 C ATOM 7327 O TYR D 141 69.798 30.405 −35.242 1.00 52.27 O ATOM 7328 CB TYR D 141 68.241 32.681 −37.124 1.00 44.35 C ATOM 7329 CG TYR D 141 67.590 31.374 −37.474 1.00 49.07 C ATOM 7330 CD1 TYR D 141 66.262 31.130 −37.159 1.00 52.39 C ATOM 7331 CD2 TYR D 141 68.316 30.363 −38.080 1.00 50.26 C ATOM 7332 CE1 TYR D 141 65.671 29.923 −37.460 1.00 53.71 C ATOM 7333 CE2 TYR D 141 67.738 29.156 −38.384 1.00 56.28 C ATOM 7334 CZ TYR D 141 66.416 28.938 −38.072 1.00 58.21 C ATOM 7335 OH TYR D 141 65.847 27.725 −38.379 1.00 64.43 O ATOM 7336 N GLN D 142 71.116 31.636 −36.579 1.00 58.51 N ATOM 7337 CA GLN D 142 72.141 30.591 −36.677 1.00 60.44 C ATOM 7338 C GLN D 142 72.748 30.266 −35.313 1.00 54.24 C ATOM 7339 O GLN D 142 73.195 29.139 −35.077 1.00 46.99 O ATOM 7340 CB GLN D 142 73.260 30.973 −37.658 1.00 44.09 C ATOM 7341 CG GLN D 142 72.833 31.082 −39.113 1.00 68.19 C ATOM 7342 CD GLN D 142 72.350 29.760 −39.693 1.00 85.43 C ATOM 7343 OE1 GLN D 142 72.414 28.719 −39.034 1.00 82.31 O ATOM 7344 NE2 GLN D 142 71.859 29.797 −40.934 1.00 82.50 N ATOM 7345 N SER D 143 72.765 31.249 −34.417 1.00 40.62 N ATOM 7346 CA SER D 143 73.425 31.055 −33.132 1.00 56.38 C ATOM 7347 C SER D 143 72.526 30.467 −32.038 1.00 57.58 C ATOM 7348 O SER D 143 73.024 29.909 −31.062 1.00 59.80 O ATOM 7349 CB SER D 143 74.105 32.346 −32.653 1.00 59.15 C ATOM 7350 OG SER D 143 73.225 33.451 −32.716 1.00 63.47 O ATOM 7351 N LEU D 144 71.210 30.573 −32.199 1.00 57.69 N ATOM 7352 CA LEU D 144 70.280 30.033 −31.199 1.00 56.25 C ATOM 7353 C LEU D 144 69.652 28.703 −31.598 1.00 55.07 C ATOM 7354 O LEU D 144 69.592 27.779 −30.791 1.00 46.13 O ATOM 7355 CB LEU D 144 69.175 31.039 −30.886 1.00 44.27 C ATOM 7356 CG LEU D 144 69.710 32.338 −30.298 1.00 60.25 C ATOM 7357 CD1 LEU D 144 68.602 33.381 −30.233 1.00 39.07 C ATOM 7358 CD2 LEU D 144 70.346 32.083 −28.930 1.00 45.81 C ATOM 7359 N MET D 145 69.172 28.608 −32.834 1.00 53.94 N ATOM 7360 CA MET D 145 68.469 27.405 −33.263 1.00 50.03 C ATOM 7361 C MET D 145 69.394 26.246 −33.597 1.00 43.48 C ATOM 7362 O MET D 145 70.256 26.345 −34.466 1.00 56.88 O ATOM 7363 CB MET D 145 67.494 27.700 −34.407 1.00 54.91 C ATOM 7364 CG MET D 145 66.151 28.273 −33.915 1.00 76.96 C ATOM 7365 SD MET D 145 64.809 27.079 −33.617 1.00 67.04 S ATOM 7366 CE MET D 145 65.706 25.525 −33.630 1.00 42.27 C ATOM 7367 N THR D 146 69.207 25.152 −32.872 1.00 34.27 N ATOM 7368 CA THR D 146 69.978 23.944 −33.069 1.00 40.34 C ATOM 7369 C THR D 146 68.995 22.789 −33.161 1.00 37.47 C ATOM 7370 O THR D 146 67.806 22.971 −32.936 1.00 47.72 O ATOM 7371 CB THR D 146 70.956 23.710 −31.902 1.00 44.17 C ATOM 7372 OG1 THR D 146 70.225 23.464 −30.691 1.00 35.16 O ATOM 7373 CG2 THR D 146 71.830 24.926 −31.708 1.00 38.19 C ATOM 7374 N ARG D 147 69.477 21.603 −33.489 1.00 37.23 N ATOM 7375 CA ARG D 147 68.595 20.457 −33.583 1.00 37.98 C ATOM 7376 C ARG D 147 68.060 20.011 −32.213 1.00 41.29 C ATOM 7377 O ARG D 147 66.903 19.602 −32.101 1.00 50.13 O ATOM 7378 CB ARG D 147 69.287 19.307 −34.325 1.00 55.09 C ATOM 7379 CG ARG D 147 69.795 19.720 −35.706 1.00 40.18 C ATOM 7380 CD ARG D 147 69.823 18.573 −36.711 1.00 49.25 C ATOM 7381 NE ARG D 147 69.794 19.107 −38.074 1.00 72.21 N ATOM 7382 CZ ARG D 147 70.865 19.554 −38.728 1.00 77.37 C ATOM 7383 NH1 ARG D 147 72.064 19.518 −38.157 1.00 54.89 N ATOM 7384 NH2 ARG D 147 70.741 20.033 −39.959 1.00 74.69 N ATOM 7385 N ALA D 148 68.887 20.089 −31.173 1.00 38.80 N ATOM 7386 CA ALA D 148 68.436 19.727 −29.837 1.00 38.10 C ATOM 7387 C ALA D 148 67.301 20.651 −29.432 1.00 38.90 C ATOM 7388 O ALA D 148 66.313 20.225 −28.824 1.00 31.80 O ATOM 7389 CB ALA D 148 69.577 19.817 −28.846 1.00 27.14 C ATOM 7390 N ARG D 149 67.456 21.921 −29.791 1.00 33.66 N ATOM 7391 CA ARG D 149 66.482 22.936 −29.451 1.00 26.23 C ATOM 7392 C ARG D 149 65.170 22.719 −30.166 1.00 37.68 C ATOM 7393 O ARG D 149 64.095 22.741 −29.548 1.00 33.18 O ATOM 7394 CB ARG D 149 67.027 24.328 −29.740 1.00 30.30 C ATOM 7395 CG ARG D 149 67.270 25.101 −28.461 1.00 30.50 C ATOM 7396 CD ARG D 149 68.158 26.307 −28.612 1.00 36.58 C ATOM 7397 NE ARG D 149 69.106 26.336 −27.505 1.00 46.07 N ATOM 7398 CZ ARG D 149 70.135 27.170 −27.410 1.00 54.25 C ATOM 7399 NH1 ARG D 149 70.351 28.079 −28.353 1.00 56.94 N ATOM 7400 NH2 ARG D 149 70.950 27.098 −26.363 1.00 55.80 N ATOM 7401 N ALA D 150 65.261 22.516 −31.476 1.00 34.90 N ATOM 7402 CA ALA D 150 64.085 22.241 −32.284 1.00 27.49 C ATOM 7403 C ALA D 150 63.256 21.081 −31.717 1.00 30.80 C ATOM 7404 O ALA D 150 62.028 21.166 −31.664 1.00 28.73 O ATOM 7405 CB ALA D 150 64.498 21.958 −33.703 1.00 27.97 C ATOM 7406 N LYS D 151 63.928 20.008 −31.296 1.00 25.88 N ATOM 7407 CA LYS D 151 63.256 18.862 −30.683 1.00 33.27 C ATOM 7408 C LYS D 151 62.529 19.238 −29.382 1.00 37.25 C ATOM 7409 O LYS D 151 61.414 18.771 −29.106 1.00 34.39 O ATOM 7410 CB LYS D 151 64.247 17.720 −30.433 1.00 31.45 C ATOM 7411 CG LYS D 151 64.693 17.047 −31.714 1.00 45.16 C ATOM 7412 CD LYS D 151 65.653 15.899 −31.466 1.00 57.07 C ATOM 7413 CE LYS D 151 66.528 15.659 −32.691 1.00 52.60 C ATOM 7414 NZ LYS D 151 67.276 14.371 −32.612 1.00 71.61 N ATOM 7415 N VAL D 152 63.160 20.081 −28.580 1.00 23.31 N ATOM 7416 CA VAL D 152 62.483 20.608 −27.411 1.00 29.69 C ATOM 7417 C VAL D 152 61.190 21.309 −27.846 1.00 28.57 C ATOM 7418 O VAL D 152 60.129 21.049 −27.286 1.00 34.22 O ATOM 7419 CB VAL D 152 63.409 21.533 −26.581 1.00 25.80 C ATOM 7420 CG1 VAL D 152 62.619 22.376 −25.607 1.00 17.42 C ATOM 7421 CG2 VAL D 152 64.415 20.701 −25.846 1.00 25.18 C ATOM 7422 N ILE D 153 61.273 22.165 −28.863 1.00 24.55 N ATOM 7423 CA ILE D 153 60.098 22.876 −29.370 1.00 24.31 C ATOM 7424 C ILE D 153 58.995 21.941 −29.887 1.00 25.84 C ATOM 7425 O ILE D 153 57.814 22.159 −29.618 1.00 25.79 O ATOM 7426 CB ILE D 153 60.471 23.871 −30.478 1.00 26.58 C ATOM 7427 CG1 ILE D 153 61.446 24.929 −29.951 1.00 21.99 C ATOM 7428 CG2 ILE D 153 59.222 24.525 −31.045 1.00 18.33 C ATOM 7429 CD1 ILE D 153 62.353 25.523 −31.018 1.00 19.47 C ATOM 7430 N ILE D 154 59.380 20.906 −30.629 1.00 23.16 N ATOM 7431 CA ILE D 154 58.435 19.889 −31.080 1.00 23.89 C ATOM 7432 C ILE D 154 57.636 19.300 −29.909 1.00 30.42 C ATOM 7433 O ILE D 154 56.410 19.194 −29.975 1.00 26.57 O ATOM 7434 CB ILE D 154 59.158 18.765 −31.859 1.00 27.64 C ATOM 7435 CG1 ILE D 154 59.411 19.221 −33.292 1.00 29.29 C ATOM 7436 CG2 ILE D 154 58.352 17.464 −31.860 1.00 18.05 C ATOM 7437 CD1 ILE D 154 60.532 18.483 −33.985 1.00 40.50 C ATOM 7438 N CYS D 155 58.336 18.939 −28.835 1.00 25.15 N ATOM 7439 CA CYS D 155 57.715 18.260 −27.701 1.00 28.64 C ATOM 7440 C CYS D 155 56.866 19.198 −26.862 1.00 27.82 C ATOM 7441 O CYS D 155 55.849 18.796 −26.298 1.00 20.58 O ATOM 7442 CB CYS D 155 58.781 17.604 −26.824 1.00 45.98 C ATOM 7443 SG CYS D 155 59.798 16.403 −27.707 1.00 65.51 S ATOM 7444 N THR D 156 57.309 20.444 −26.763 1.00 26.79 N ATOM 7445 CA THR D 156 56.534 21.479 −26.101 1.00 28.92 C ATOM 7446 C THR D 156 55.198 21.612 −26.829 1.00 23.27 C ATOM 7447 O THR D 156 54.148 21.678 −26.198 1.00 19.47 O ATOM 7448 CB THR D 156 57.314 22.814 −26.092 1.00 23.83 C ATOM 7449 OG1 THR D 156 58.552 22.621 −25.408 1.00 30.54 O ATOM 7450 CG2 THR D 156 56.548 23.909 −25.395 1.00 17.72 C ATOM 7451 N VAL D 157 55.251 21.620 −28.159 1.00 22.30 N ATOM 7452 CA VAL D 157 54.044 21.641 −28.984 1.00 20.58 C ATOM 7453 C VAL D 157 53.124 20.439 −28.763 1.00 20.63 C ATOM 7454 O VAL D 157 51.934 20.615 −28.549 1.00 24.08 O ATOM 7455 CB VAL D 157 54.381 21.752 −30.461 1.00 17.06 C ATOM 7456 CG1 VAL D 157 53.241 21.228 −31.292 1.00 27.89 C ATOM 7457 CG2 VAL D 157 54.668 23.190 −30.818 1.00 22.07 C ATOM 7458 N TRP D 158 53.668 19.226 −28.802 1.00 20.87 N ATOM 7459 CA TRP D 158 52.888 18.028 −28.503 1.00 19.71 C ATOM 7460 C TRP D 158 52.324 18.005 −27.058 1.00 27.18 C ATOM 7461 O TRP D 158 51.195 17.548 −26.819 1.00 21.35 O ATOM 7462 CB TRP D 158 53.708 16.767 −28.794 1.00 18.69 C ATOM 7463 CG TRP D 158 53.765 16.424 −30.259 1.00 33.87 C ATOM 7464 CD1 TRP D 158 54.735 16.786 −31.154 1.00 31.36 C ATOM 7465 CD2 TRP D 158 52.808 15.655 −31.000 1.00 35.65 C ATOM 7466 NE1 TRP D 158 54.439 16.296 −32.402 1.00 25.97 N ATOM 7467 CE2 TRP D 158 53.262 15.600 −32.339 1.00 30.33 C ATOM 7468 CE3 TRP D 158 51.610 15.013 −30.664 1.00 30.95 C ATOM 7469 CZ2 TRP D 158 52.564 14.926 −33.340 1.00 30.21 C ATOM 7470 CZ3 TRP D 158 50.917 14.346 −31.662 1.00 41.29 C ATOM 7471 CH2 TRP D 158 51.400 14.308 −32.989 1.00 32.18 C ATOM 7472 N ALA D 159 53.114 18.495 −26.102 1.00 26.63 N ATOM 7473 CA ALA D 159 52.671 18.640 −24.721 1.00 17.00 C ATOM 7474 C ALA D 159 51.461 19.554 −24.621 1.00 22.89 C ATOM 7475 O ALA D 159 50.405 19.148 −24.128 1.00 26.91 O ATOM 7476 CB ALA D 159 53.780 19.196 −23.880 1.00 20.16 C ATOM 7477 N ILE D 160 51.622 20.796 −25.068 1.00 17.90 N ATOM 7478 CA ILE D 160 50.525 21.754 −25.083 1.00 20.21 C ATOM 7479 C ILE D 160 49.311 21.162 −25.774 1.00 28.21 C ATOM 7480 O ILE D 160 48.170 21.398 −25.367 1.00 26.79 O ATOM 7481 CB ILE D 160 50.908 23.044 −25.798 1.00 25.44 C ATOM 7482 CG1 ILE D 160 51.961 23.787 −24.971 1.00 28.15 C ATOM 7483 CG2 ILE D 160 49.678 23.902 −26.028 1.00 18.32 C ATOM 7484 CD1 ILE D 160 52.618 24.945 −25.693 1.00 22.66 C ATOM 7485 N SER D 161 49.562 20.376 −26.813 1.00 24.17 N ATOM 7486 CA SER D 161 48.483 19.755 −27.565 1.00 24.04 C ATOM 7487 C SER D 161 47.699 18.706 −26.774 1.00 19.64 C ATOM 7488 O SER D 161 46.482 18.756 −26.764 1.00 26.32 O ATOM 7489 CB SER D 161 49.010 19.184 −28.873 1.00 28.01 C ATOM 7490 OG SER D 161 49.485 20.230 −29.702 1.00 36.67 O ATOM 7491 N ALA D 162 48.376 17.758 −26.130 1.00 18.53 N ATOM 7492 CA ALA D 162 47.695 16.808 −25.244 1.00 25.97 C ATOM 7493 C ALA D 162 46.943 17.508 −24.075 1.00 30.96 C ATOM 7494 O ALA D 162 45.828 17.119 −23.696 1.00 22.01 O ATOM 7495 CB ALA D 162 48.681 15.782 −24.712 1.00 17.14 C ATOM 7496 N LEU D 163 47.565 18.536 −23.505 1.00 21.69 N ATOM 7497 CA LEU D 163 46.905 19.377 −22.523 1.00 25.12 C ATOM 7498 C LEU D 163 45.494 19.829 −22.939 1.00 24.24 C ATOM 7499 O LEU D 163 44.526 19.517 −22.262 1.00 22.72 O ATOM 7500 CB LEU D 163 47.761 20.609 −22.237 1.00 28.83 C ATOM 7501 CG LEU D 163 47.265 21.453 −21.067 1.00 19.49 C ATOM 7502 CD1 LEU D 163 47.125 20.550 −19.865 1.00 14.86 C ATOM 7503 CD2 LEU D 163 48.207 22.610 −20.795 1.00 15.19 C ATOM 7504 N VAL D 164 45.389 20.581 −24.038 1.00 29.89 N ATOM 7505 CA VAL D 164 44.100 21.124 −24.501 1.00 33.15 C ATOM 7506 C VAL D 164 43.209 20.125 −25.259 1.00 28.57 C ATOM 7507 O VAL D 164 42.114 20.490 −25.702 1.00 31.65 O ATOM 7508 CB VAL D 164 44.263 22.392 −25.387 1.00 28.92 C ATOM 7509 CG1 VAL D 164 45.253 23.344 −24.776 1.00 19.27 C ATOM 7510 CG2 VAL D 164 44.671 22.015 −26.816 1.00 20.60 C ATOM 7511 N SER D 165 43.665 18.881 −25.401 1.00 19.24 N ATOM 7512 CA SER D 165 42.882 17.870 −26.103 1.00 19.68 C ATOM 7513 C SER D 165 42.556 16.605 −25.293 1.00 27.11 C ATOM 7514 O SER D 165 41.390 16.217 −25.195 1.00 38.00 O ATOM 7515 CB SER D 165 43.540 17.509 −27.428 1.00 26.61 C ATOM 7516 OG SER D 165 44.804 16.934 −27.195 1.00 42.66 O ATOM 7517 N PHE D 166 43.558 15.956 −24.712 1.00 25.41 N ATOM 7518 CA PHE D 166 43.291 14.833 −23.805 1.00 32.72 C ATOM 7519 C PHE D 166 42.580 15.218 −22.501 1.00 32.78 C ATOM 7520 O PHE D 166 41.643 14.552 −22.063 1.00 28.27 O ATOM 7521 CB PHE D 166 44.587 14.132 −23.426 1.00 34.98 C ATOM 7522 CG PHE D 166 45.151 13.306 −24.508 1.00 37.78 C ATOM 7523 CD1 PHE D 166 46.526 13.128 −24.615 1.00 37.93 C ATOM 7524 CD2 PHE D 166 44.312 12.710 −25.432 1.00 27.58 C ATOM 7525 CE1 PHE D 166 47.054 12.347 −25.630 1.00 48.10 C ATOM 7526 CE2 PHE D 166 44.823 11.929 −26.445 1.00 36.47 C ATOM 7527 CZ PHE D 166 46.196 11.746 −26.553 1.00 48.52 C ATOM 7528 N LEU D 167 43.050 16.284 −21.869 1.00 31.22 N ATOM 7529 CA LEU D 167 42.644 16.578 −20.507 1.00 24.27 C ATOM 7530 C LEU D 167 41.205 17.030 −20.286 1.00 22.52 C ATOM 7531 O LEU D 167 40.596 16.625 −19.310 1.00 31.01 O ATOM 7532 CB LEU D 167 43.650 17.505 −19.837 1.00 29.06 C ATOM 7533 CG LEU D 167 44.659 16.667 −19.043 1.00 32.36 C ATOM 7534 CD1 LEU D 167 45.995 17.351 −18.961 1.00 28.14 C ATOM 7535 CD2 LEU D 167 44.103 16.366 −17.655 1.00 30.10 C ATOM 7536 N PRO D 168 40.654 17.871 −21.172 1.00 27.00 N ATOM 7537 CA PRO D 168 39.216 18.153 −21.034 1.00 25.38 C ATOM 7538 C PRO D 168 38.318 16.939 −21.346 1.00 27.51 C ATOM 7539 O PRO D 168 37.169 16.876 −20.891 1.00 23.43 O ATOM 7540 CB PRO D 168 38.986 19.276 −22.041 1.00 20.69 C ATOM 7541 CG PRO D 168 40.330 19.950 −22.144 1.00 25.76 C ATOM 7542 CD PRO D 168 41.310 18.819 −22.089 1.00 27.16 C ATOM 7543 N ILE D 169 38.840 15.975 −22.098 1.00 22.26 N ATOM 7544 CA ILE D 169 38.081 14.772 −22.374 1.00 19.56 C ATOM 7545 C ILE D 169 38.069 13.833 −21.179 1.00 23.23 C ATOM 7546 O ILE D 169 37.032 13.274 −20.832 1.00 29.55 O ATOM 7547 CB ILE D 169 38.552 14.068 −23.660 1.00 27.64 C ATOM 7548 CG1 ILE D 169 38.224 14.961 −24.858 1.00 27.07 C ATOM 7549 CG2 ILE D 169 37.887 12.701 −23.820 1.00 20.45 C ATOM 7550 CD1 ILE D 169 37.779 14.209 −26.070 1.00 33.78 C ATOM 7551 N MET D 170 39.208 13.676 −20.523 1.00 29.38 N ATOM 7552 CA MET D 170 39.241 12.841 −19.324 1.00 31.28 C ATOM 7553 C MET D 170 38.500 13.438 −18.100 1.00 30.64 C ATOM 7554 O MET D 170 38.050 12.701 −17.221 1.00 33.24 O ATOM 7555 CB MET D 170 40.671 12.335 −19.009 1.00 30.31 C ATOM 7556 CG MET D 170 41.823 13.274 −19.351 1.00 31.99 C ATOM 7557 SD MET D 170 43.429 12.470 −19.662 1.00 46.70 S ATOM 7558 CE MET D 170 43.507 11.146 −18.459 1.00 21.11 C ATOM 7559 N MET D 171 38.340 14.760 −18.062 1.00 27.69 N ATOM 7560 CA MET D 171 37.560 15.401 −17.003 1.00 24.80 C ATOM 7561 C MET D 171 36.121 15.645 −17.447 1.00 30.85 C ATOM 7562 O MET D 171 35.359 16.342 −16.774 1.00 28.17 O ATOM 7563 CB MET D 171 38.204 16.717 −16.594 1.00 23.05 C ATOM 7564 CG MET D 171 39.607 16.556 −16.038 1.00 30.00 C ATOM 7565 SD MET D 171 40.415 18.164 −15.938 1.00 36.62 S ATOM 7566 CE MET D 171 39.413 18.900 −14.646 1.00 67.55 C ATOM 7567 N HIS D 172 35.765 15.090 −18.599 1.00 25.40 N ATOM 7568 CA HIS D 172 34.403 15.170 −19.111 1.00 26.32 C ATOM 7569 C HIS D 172 33.864 16.588 −19.319 1.00 25.68 C ATOM 7570 O HIS D 172 32.661 16.804 −19.260 1.00 28.54 O ATOM 7571 CB HIS D 172 33.465 14.387 −18.201 1.00 22.45 C ATOM 7572 CG HIS D 172 33.946 13.005 −17.879 1.00 26.46 C ATOM 7573 ND1 HIS D 172 33.427 11.879 −18.483 1.00 24.98 N ATOM 7574 CD2 HIS D 172 34.884 12.563 −17.010 1.00 28.11 C ATOM 7575 CE1 HIS D 172 34.031 10.808 −18.006 1.00 24.39 C ATOM 7576 NE2 HIS D 172 34.917 11.191 −17.104 1.00 23.42 N ATOM 7577 N TRP D 173 34.746 17.541 −19.601 1.00 25.47 N ATOM 7578 CA TRP D 173 34.342 18.939 −19.746 1.00 26.74 C ATOM 7579 C TRP D 173 33.500 19.165 −20.988 1.00 29.81 C ATOM 7580 O TRP D 173 32.887 20.217 −21.157 1.00 33.48 O ATOM 7581 CB TRP D 173 35.573 19.839 −19.800 1.00 24.06 C ATOM 7582 CG TRP D 173 36.233 20.044 −18.466 1.00 28.36 C ATOM 7583 CD1 TRP D 173 36.002 19.343 −17.311 1.00 22.02 C ATOM 7584 CD2 TRP D 173 37.255 21.004 −18.157 1.00 28.26 C ATOM 7585 NE1 TRP D 173 36.805 19.825 −16.303 1.00 21.74 N ATOM 7586 CE2 TRP D 173 37.582 20.843 −16.797 1.00 27.98 C ATOM 7587 CE3 TRP D 173 37.918 21.989 −18.896 1.00 23.06 C ATOM 7588 CZ2 TRP D 173 38.548 21.627 −16.166 1.00 24.59 C ATOM 7589 CZ3 TRP D 173 38.872 22.766 −18.263 1.00 25.97 C ATOM 7590 CH2 TRP D 173 39.176 22.582 −16.916 1.00 19.52 C ATOM 7591 N TRP D 174 33.463 18.163 −21.854 1.00 26.71 N ATOM 7592 CA TRP D 174 32.848 18.315 −23.161 1.00 23.52 C ATOM 7593 C TRP D 174 31.373 17.942 −23.168 1.00 29.29 C ATOM 7594 O TRP D 174 30.632 18.357 −24.063 1.00 29.53 O ATOM 7595 CB TRP D 174 33.585 17.458 −24.183 1.00 22.03 C ATOM 7596 CG TRP D 174 33.575 16.004 −23.841 1.00 22.53 C ATOM 7597 CD1 TRP D 174 34.394 15.370 −22.956 1.00 22.59 C ATOM 7598 CD2 TRP D 174 32.699 15.001 −24.367 1.00 20.26 C ATOM 7599 NE1 TRP D 174 34.088 14.032 −22.900 1.00 19.03 N ATOM 7600 CE2 TRP D 174 33.051 13.779 −23.756 1.00 17.62 C ATOM 7601 CE3 TRP D 174 31.651 15.017 −25.287 1.00 20.15 C ATOM 7602 CZ2 TRP D 174 32.407 12.588 −24.048 1.00 17.06 C ATOM 7603 CZ3 TRP D 174 31.013 13.830 −25.573 1.00 21.16 C ATOM 7604 CH2 TRP D 174 31.396 12.631 −24.959 1.00 16.11 C ATOM 7605 N ARG D 175 30.944 17.165 −22.175 1.00 30.92 N ATOM 7606 CA ARG D 175 29.594 16.576 −22.197 1.00 34.78 C ATOM 7607 C ARG D 175 28.437 17.574 −22.066 1.00 34.17 C ATOM 7608 O ARG D 175 28.567 18.617 −21.431 1.00 28.59 O ATOM 7609 CB ARG D 175 29.467 15.468 −21.152 1.00 17.96 C ATOM 7610 CG ARG D 175 30.408 14.321 −21.395 1.00 18.10 C ATOM 7611 CD ARG D 175 30.020 13.142 −20.554 1.00 23.60 C ATOM 7612 NE ARG D 175 31.094 12.168 −20.400 1.00 23.40 N ATOM 7613 CZ ARG D 175 31.252 11.094 −21.172 1.00 26.93 C ATOM 7614 NH1 ARG D 175 30.406 10.861 −22.165 1.00 28.77 N ATOM 7615 NH2 ARG D 175 32.255 10.252 −20.954 1.00 24.08 N ATOM 7616 N ASP D 176 27.304 17.238 −22.682 1.00 39.51 N ATOM 7617 CA ASP D 176 26.106 18.063 −22.584 1.00 39.91 C ATOM 7618 C ASP D 176 25.069 17.473 −21.617 1.00 34.58 C ATOM 7619 O ASP D 176 25.210 16.347 −21.137 1.00 30.48 O ATOM 7620 CB ASP D 176 25.494 18.285 −23.967 1.00 38.79 C ATOM 7621 CG ASP D 176 24.764 19.625 −24.082 1.00 59.31 C ATOM 7622 OD1 ASP D 176 24.712 20.390 −23.089 1.00 51.38 O ATOM 7623 OD2 ASP D 176 24.245 19.914 −25.180 1.00 65.27 O ATOM 7624 N GLU D 177 24.035 18.252 −21.322 1.00 43.89 N ATOM 7625 CA GLU D 177 22.994 17.810 −20.402 1.00 49.30 C ATOM 7626 C GLU D 177 21.768 17.206 −21.126 1.00 50.47 C ATOM 7627 O GLU D 177 21.092 16.340 −20.569 1.00 49.84 O ATOM 7628 CB GLU D 177 22.579 18.949 −19.461 1.00 47.65 C ATOM 7629 CG GLU D 177 23.735 19.637 −18.725 1.00 55.47 C ATOM 7630 CD GLU D 177 24.302 18.807 −17.573 1.00 82.15 C ATOM 7631 OE1 GLU D 177 23.901 17.626 −17.430 1.00 81.01 O ATOM 7632 OE2 GLU D 177 25.148 19.338 −16.813 1.00 59.73 O ATOM 7633 N ASP D 178 21.507 17.646 −22.360 1.00 46.36 N ATOM 7634 CA ASP D 178 20.410 17.117 −23.199 1.00 58.43 C ATOM 7635 C ASP D 178 20.188 15.602 −23.170 1.00 57.78 C ATOM 7636 O ASP D 178 21.142 14.821 −23.216 1.00 48.31 O ATOM 7637 CB ASP D 178 20.597 17.530 −24.662 1.00 56.35 C ATOM 7638 CG ASP D 178 20.395 19.012 −24.878 1.00 98.69 C ATOM 7639 OD1 ASP D 178 20.173 19.735 −23.879 1.00 105.79 O ATOM 7640 OD2 ASP D 178 20.461 19.453 −26.047 1.00 118.01 O ATOM 7641 N PRO D 179 18.911 15.183 −23.160 1.00 59.03 N ATOM 7642 CA PRO D 179 18.595 13.754 −23.098 1.00 55.25 C ATOM 7643 C PRO D 179 19.170 13.067 −24.332 1.00 49.95 C ATOM 7644 O PRO D 179 19.646 11.929 −24.286 1.00 39.90 O ATOM 7645 CB PRO D 179 17.058 13.726 −23.144 1.00 55.74 C ATOM 7646 CG PRO D 179 16.608 15.162 −23.004 1.00 53.23 C ATOM 7647 CD PRO D 179 17.730 15.998 −23.491 1.00 53.75 C ATOM 7648 N GLN D 180 19.117 13.786 −25.445 1.00 46.60 N ATOM 7649 CA GLN D 180 19.661 13.295 −26.692 1.00 53.46 C ATOM 7650 C GLN D 180 21.134 12.993 −26.495 1.00 44.53 C ATOM 7651 O GLN D 180 21.580 11.876 −26.744 1.00 39.60 O ATOM 7652 CB GLN D 180 19.456 14.333 −27.794 1.00 65.36 C ATOM 7653 CG GLN D 180 17.988 14.706 −28.028 1.00 76.49 C ATOM 7654 CD GLN D 180 17.243 13.690 −28.881 1.00 87.77 C ATOM 7655 OE1 GLN D 180 17.837 13.001 −29.715 1.00 86.58 O ATOM 7656 NE2 GLN D 180 15.931 13.601 −28.681 1.00 89.58 N ATOM 7657 N ALA D 181 21.878 13.990 −26.023 1.00 48.39 N ATOM 7658 CA ALA D 181 23.277 13.798 −25.644 1.00 40.56 C ATOM 7659 C ALA D 181 23.419 12.624 −24.682 1.00 40.69 C ATOM 7660 O ALA D 181 24.271 11.754 −24.862 1.00 29.47 O ATOM 7661 CB ALA D 181 23.824 15.057 −25.004 1.00 39.08 C ATOM 7662 N LEU D 182 22.563 12.606 −23.663 1.00 38.04 N ATOM 7663 CA LEU D 182 22.621 11.592 −22.617 1.00 34.04 C ATOM 7664 C LEU D 182 22.414 10.157 −23.122 1.00 31.64 C ATOM 7665 O LEU D 182 23.108 9.237 −22.698 1.00 32.96 O ATOM 7666 CB LEU D 182 21.651 11.935 −21.478 1.00 33.24 C ATOM 7667 CG LEU D 182 22.020 13.161 −20.627 1.00 32.58 C ATOM 7668 CD1 LEU D 182 21.097 13.285 −19.460 1.00 31.48 C ATOM 7669 CD2 LEU D 182 23.449 13.069 −20.129 1.00 35.88 C ATOM 7670 N LYS D 183 21.480 9.960 −24.037 1.00 35.19 N ATOM 7671 CA LYS D 183 21.309 8.637 −24.635 1.00 42.64 C ATOM 7672 C LYS D 183 22.533 8.195 −25.457 1.00 43.62 C ATOM 7673 O LYS D 183 22.888 7.014 −25.463 1.00 37.74 O ATOM 7674 CB LYS D 183 20.007 8.575 −25.434 1.00 42.72 C ATOM 7675 CG LYS D 183 18.810 8.991 −24.573 1.00 66.04 C ATOM 7676 CD LYS D 183 17.460 8.652 −25.186 1.00 75.45 C ATOM 7677 CE LYS D 183 16.329 9.201 −24.328 1.00 68.06 C ATOM 7678 NZ LYS D 183 14.993 8.774 −24.818 1.00 79.76 N ATOM 7679 N CYS D 184 23.191 9.146 −26.122 1.00 38.11 N ATOM 7680 CA CYS D 184 24.459 8.871 −26.801 1.00 36.49 C ATOM 7681 C CYS D 184 25.565 8.479 −25.814 1.00 35.00 C ATOM 7682 O CYS D 184 26.476 7.722 −26.158 1.00 42.57 O ATOM 7683 CB CYS D 184 24.913 10.084 −27.620 1.00 41.76 C ATOM 7684 SG CYS D 184 26.088 9.685 −28.938 1.00 77.84 S ATOM 7685 N TYR D 185 25.497 9.000 −24.594 1.00 25.67 N ATOM 7686 CA TYR D 185 26.461 8.615 −23.583 1.00 27.83 C ATOM 7687 C TYR D 185 26.204 7.210 −23.052 1.00 35.95 C ATOM 7688 O TYR D 185 27.141 6.524 −22.656 1.00 40.48 O ATOM 7689 CB TYR D 185 26.529 9.631 −22.441 1.00 28.32 C ATOM 7690 CG TYR D 185 26.846 11.030 −22.906 1.00 29.33 C ATOM 7691 CD1 TYR D 185 27.589 11.240 −24.060 1.00 21.87 C ATOM 7692 CD2 TYR D 185 26.407 12.142 −22.191 1.00 31.54 C ATOM 7693 CE1 TYR D 185 27.877 12.508 −24.504 1.00 17.57 C ATOM 7694 CE2 TYR D 185 26.700 13.421 −22.616 1.00 30.13 C ATOM 7695 CZ TYR D 185 27.440 13.598 −23.778 1.00 30.22 C ATOM 7696 OH TYR D 185 27.740 14.869 −24.220 1.00 31.93 O ATOM 7697 N GLN D 186 24.948 6.765 −23.055 1.00 39.80 N ATOM 7698 CA GLN D 186 24.671 5.369 −22.681 1.00 41.49 C ATOM 7699 C GLN D 186 24.934 4.346 −23.795 1.00 39.37 C ATOM 7700 O GLN D 186 25.522 3.303 −23.534 1.00 38.57 O ATOM 7701 CB GLN D 186 23.291 5.168 −22.026 1.00 34.03 C ATOM 7702 CG GLN D 186 22.262 6.257 −22.265 1.00 51.03 C ATOM 7703 CD GLN D 186 20.969 6.025 −21.471 1.00 61.24 C ATOM 7704 OE1 GLN D 186 20.943 5.243 −20.513 1.00 62.55 O ATOM 7705 NE2 GLN D 186 19.896 6.709 −21.869 1.00 50.15 N ATOM 7706 N ASP D 187 24.526 4.645 −25.028 1.00 38.37 N ATOM 7707 CA ASP D 187 24.813 3.740 −26.139 1.00 41.84 C ATOM 7708 C ASP D 187 26.320 3.684 −26.403 1.00 43.32 C ATOM 7709 O ASP D 187 26.957 4.711 −26.677 1.00 40.88 O ATOM 7710 CB ASP D 187 24.055 4.155 −27.410 1.00 37.79 C ATOM 7711 CG ASP D 187 23.886 3.000 −28.410 1.00 51.75 C ATOM 7712 OD1 ASP D 187 24.559 1.948 −28.267 1.00 51.05 O ATOM 7713 OD2 ASP D 187 23.071 3.145 −29.347 1.00 49.88 O ATOM 7714 N PRO D 188 26.903 2.481 −26.292 1.00 38.36 N ATOM 7715 CA PRO D 188 28.322 2.295 −26.595 1.00 43.95 C ATOM 7716 C PRO D 188 28.478 2.295 −28.100 1.00 46.22 C ATOM 7717 O PRO D 188 29.540 2.638 −28.626 1.00 51.98 O ATOM 7718 CB PRO D 188 28.632 0.901 −26.036 1.00 34.89 C ATOM 7719 CG PRO D 188 27.449 0.515 −25.218 1.00 43.85 C ATOM 7720 CD PRO D 188 26.283 1.245 −25.806 1.00 39.53 C ATOM 7721 N GLY D 189 27.401 1.917 −28.782 1.00 35.98 N ATOM 7722 CA GLY D 189 27.369 1.893 −30.230 1.00 29.99 C ATOM 7723 C GLY D 189 27.192 3.271 −30.826 1.00 33.06 C ATOM 7724 O GLY D 189 27.220 3.438 −32.041 1.00 42.62 O ATOM 7725 N CYS D 190 26.998 4.269 −29.975 1.00 36.26 N ATOM 7726 CA CYS D 190 26.980 5.642 −30.450 1.00 36.63 C ATOM 7727 C CYS D 190 28.260 6.372 −30.048 1.00 36.49 C ATOM 7728 O CYS D 190 28.602 6.474 −28.866 1.00 36.99 O ATOM 7729 CB CYS D 190 25.754 6.390 −29.943 1.00 25.70 C ATOM 7730 SG CYS D 190 25.842 8.157 −30.296 1.00 52.32 S ATOM 7731 N CYS D 191 28.972 6.869 −31.047 1.00 32.07 N ATOM 7732 CA CYS D 191 30.217 7.571 −30.805 1.00 33.08 C ATOM 7733 C CYS D 191 30.170 8.942 −31.430 1.00 31.14 C ATOM 7734 O CYS D 191 31.041 9.312 −32.211 1.00 33.71 O ATOM 7735 CB CYS D 191 31.417 6.808 −31.367 1.00 30.22 C ATOM 7736 SG CYS D 191 32.981 7.535 −30.803 1.00 43.00 S ATOM 7737 N ASP D 192 29.137 9.689 −31.082 1.00 26.62 N ATOM 7738 CA ASP D 192 28.949 11.021 −31.617 1.00 29.40 C ATOM 7739 C ASP D 192 29.511 12.048 −30.651 1.00 35.64 C ATOM 7740 O ASP D 192 29.383 11.930 −29.423 1.00 32.14 O ATOM 7741 CB ASP D 192 27.466 11.265 −31.903 1.00 39.75 C ATOM 7742 CG ASP D 192 26.842 10.151 −32.764 1.00 70.76 C ATOM 7743 OD1 ASP D 192 27.600 9.374 −33.398 1.00 61.18 O ATOM 7744 OD2 ASP D 192 25.590 10.048 −32.803 1.00 77.41 O ATOM 7745 N PHE D 193 30.165 13.050 −31.212 1.00 27.86 N ATOM 7746 CA PHE D 193 30.846 14.032 −30.389 1.00 34.78 C ATOM 7747 C PHE D 193 29.871 15.165 −30.119 1.00 34.95 C ATOM 7748 O PHE D 193 30.040 16.284 −30.623 1.00 29.04 O ATOM 7749 CB PHE D 193 32.135 14.511 −31.068 1.00 28.13 C ATOM 7750 CG PHE D 193 33.109 15.159 −30.138 1.00 22.65 C ATOM 7751 CD1 PHE D 193 33.233 14.729 −28.824 1.00 29.17 C ATOM 7752 CD2 PHE D 193 33.921 16.194 −30.579 1.00 21.58 C ATOM 7753 CE1 PHE D 193 34.150 15.344 −27.948 1.00 32.98 C ATOM 7754 CE2 PHE D 193 34.834 16.806 −29.722 1.00 28.32 C ATOM 7755 CZ PHE D 193 34.955 16.384 −28.404 1.00 19.52 C ATOM 7756 N VAL D 194 28.837 14.831 −29.337 1.00 32.39 N ATOM 7757 CA VAL D 194 27.814 15.776 −28.891 1.00 31.06 C ATOM 7758 C VAL D 194 28.337 16.523 −27.670 1.00 28.02 C ATOM 7759 O VAL D 194 28.441 15.964 −26.586 1.00 30.42 O ATOM 7760 CB VAL D 194 26.505 .15.054 −28.486 1.00 35.21 C ATOM 7761 CG1 VAL D 194 25.326 16.001 −28.591 1.00 30.22 C ATOM 7762 CG2 VAL D 194 26.279 13.809 −29.338 1.00 33.68 C ATOM 7763 N THR D 195 28.670 17.788 −27.840 1.00 24.75 N ATOM 7764 CA THR D 195 29.314 18.506 −26.757 1.00 33.18 C ATOM 7765 C THR D 195 28.457 19.680 −26.336 1.00 28.23 C ATOM 7766 O THR D 195 27.494 20.023 −27.005 1.00 28.87 O ATOM 7767 CB THR D 195 30.738 18.983 −27.161 1.00 35.95 C ATOM 7768 OG1 THR D 195 30.649 20.103 −28.050 1.00 34.83 O ATOM 7769 CG2 THR D 195 31.507 17.857 −27.854 1.00 28.62 C ATOM 7770 N ASN D 196 28.803 20.294 −25.218 1.00 31.98 N ATOM 7771 CA ASN D 196 28.109 21.497 −24.798 1.00 31.91 C ATOM 7772 C ASN D 196 28.638 22.714 −25.577 1.00 32.87 C ATOM 7773 O ASN D 196 29.750 22.672 −26.123 1.00 29.48 O ATOM 7774 CB ASN D 196 28.208 21.663 −23.281 1.00 29.86 C ATOM 7775 CG ASN D 196 29.638 21.826 −22.791 1.00 26.56 C ATOM 7776 OD1 ASN D 196 30.243 22.883 −22.955 1.00 25.52 O ATOM 7777 ND2 ASN D 196 30.164 20.797 −22.151 1.00 26.89 N ATOM 7778 N ARG D 197 27.839 23.776 −25.664 1.00 26.82 N ATOM 7779 CA ARG D 197 28.227 24.950 −26.450 1.00 24.80 C ATOM 7780 C ARG D 197 29.503 25.632 −25.933 1.00 28.25 C ATOM 7781 O ARG D 197 30.349 26.074 −26.729 1.00 27.93 O ATOM 7782 CB ARG D 197 27.081 25.966 −26.562 1.00 23.60 C ATOM 7783 CG ARG D 197 25.756 25.397 −27.060 1.00 36.35 C ATOM 7784 CD ARG D 197 24.745 26.516 −27.305 1.00 47.96 C ATOM 7785 NE ARG D 197 23.400 26.025 −27.622 1.00 74.96 N ATOM 7786 CZ ARG D 197 22.375 26.808 −27.969 1.00 97.26 C ATOM 7787 NH1 ARG D 197 22.529 28.127 −28.053 1.00 89.57 N ATOM 7788 NH2 ARG D 197 21.187 26.278 −28.238 1.00 99.42 N ATOM 7789 N ALA D 198 29.643 25.714 −24.608 1.00 25.83 N ATOM 7790 CA ALA D 198 30.849 26.276 −23.992 1.00 27.91 C ATOM 7791 C ALA D 198 32.099 25.597 −24.537 1.00 29.61 C ATOM 7792 O ALA D 198 32.997 26.254 −25.060 1.00 27.15 O ATOM 7793 CB ALA D 198 30.801 26.142 −22.484 1.00 20.54 C ATOM 7794 N TYR D 199 32.144 24.275 −24.411 1.00 26.38. N ATOM 7795 CA TYR D 199 33.279 23.506 −24.870 1.00 21.80 C ATOM 7796 C TYR D 199 33.487 23.659 −26.370 1.00 27.77 C ATOM 7797 O TYR D 199 34.593 23.934 −26.829 1.00 25.65 O ATOM 7798 CB TYR D 199 33.106 22.031 −24.521 1.00 23.55 C ATOM 7799 CG TYR D 199 34.192 21.178 −25.132 1.00 29.28 C ATOM 7800 CD1 TYR D 199 35.413 20.986 −24.481 1.00 26.04 C ATOM 7801 CD2 TYR D 199 34.014 20.595 −26.379 1.00 28.10 C ATOM 7802 CE1 TYR D 199 36.401 20.214 −25.045 1.00 22.24 C ATOM 7803 CE2 TYR D 199 34.999 19.827 −26.950 1.00 30.43 C ATOM 7804 CZ TYR D 199 36.189 19.638 −26.283 1.00 23.00 C ATOM 7805 OH TYR D 199 37.154 18.868 −26.879 1.00 21.93 O ATOM 7806 N ALA D 200 32.415 23.476 −27.130 1.00 31.39 N ATOM 7807 CA ALA D 200 32.507 23.531 −28.573 1.00 24.70 C ATOM 7808 C ALA D 200 33.201 24.820 −29.026 1.00 28.48 C ATOM 7809 O ALA D 200 34.113 24.779 −29.845 1.00 32.06 O ATOM 7810 CB ALA D 200 31.134 23.399 −29.197 1.00 24.71 C ATOM 7811 N ILE D 201 32.788 25.961 −28.489 1.00 23.38 N ATOM 7812 CA ILE D 201 33.410 27.224 −28.873 1.00 23.66 C ATOM 7813 C ILE D 201 34.849 27.361 −28.378 1.00 30.86 C ATOM 7814 O ILE D 201 35.738 27.769 −29.116 1.00 32.71 O ATOM 7815 CB ILE D 201 32.605 28.420 −28.367 1.00 31.04 C ATOM 7816 CG1 ILE D 201 31.334 28.580 −29.209 1.00 30.75 C ATOM 7817 CG2 ILE D 201 33.468 29.687 −28.377 1.00 18.04 C ATOM 7818 CD1 ILE D 201 30.307 29.492 −28.582 1.00 30.83 C ATOM 7819 N ALA D 202 35.081 27.015 −27.121 1.00 33.20 N ATOM 7820 CA ALA D 202 36.397 27.184 −26.522 1.00 31.65 C ATOM 7821 C ALA D 202 37.460 26.281 −27.152 1.00 30.14 C ATOM 7822 O ALA D 202 38.543 26.745 −27.506 1.00 27.71 O ATOM 7823 CB ALA D 202 36.326 26.975 −25.006 1.00 25.03 C ATOM 7824 N SER D 203 37.149 25.000 −27.295 1.00 25.50 N ATOM 7825 CA SER D 203 38.127 24.067 −27.824 1.00 30.78 C ATOM 7826 C SER D 203 38.459 24.391 −29.267 1.00 32.08 C ATOM 7827 O SER D 203 39.520 24.011 −29.766 1.00 28.24 O ATOM 7828 CB SER D 203 37.637 22.625 −27.706 1.00 31.60 C ATOM 7829 OG SER D 203 36.694 22.337 −28.706 1.00 29.65 O ATOM 7830 N SER D 204 37.552 25.107 −29.922 1.00 25.47 N ATOM 7831 CA SER D 204 37.737 25.498 −31.308 1.00 29.15 C ATOM 7832 C SER D 204 38.580 26.763 −31.444 1.00 27.51 C ATOM 7833 O SER D 204 39.483 26.837 −32.270 1.00 29.51 O ATOM 7834 CB SER D 204 36.380 25.681 −31.973 1.00 28.56 C ATOM 7835 OG SER D 204 35.663 24.463 −31.915 1.00 36.73 O ATOM 7836 N ILE D 205 38.265 27.762 −30.641 1.00 28.55 N ATOM 7837 CA ILE D 205 39.091 28.950 −30.549 1.00 29.74 C ATOM 7838 C ILE D 205 40.528 28.557 −30.204 1.00 33.12 C ATOM 7839 O ILE D 205 41.489 29.091 −30.757 1.00 32.89 O ATOM 7840 CB ILE D 205 38.531 29.902 −29.476 1.00 33.98 C ATOM 7841 CG1 ILE D 205 37.400 30.736 −30.071 1.00 37.99 C ATOM 7842 CG2 ILE D 205 39.610 30.813 −28.918 1.00 29.96 C ATOM 7843 CD1 ILE D 205 36.569 31.463 −29.036 1.00 30.28 C ATOM 7844 N ILE D 206 40.660 27.587 −29.310 1.00 31.42 N ATOM 7845 CA ILE D 206 41.956 27.220 −28.737 1.00 31.08 C ATOM 7846 C ILE D 206 42.779 26.191 −29.524 1.00 30.42 C ATOM 7847 O ILE D 206 44.007 26.238 −29.492 1.00 33.32 O ATOM 7848 CB ILE D 206 41.790 26.776 −27.256 1.00 30.45 C ATOM 7849 CG1 ILE D 206 41.945 27.991 −26.339 1.00 30.34 C ATOM 7850 CG2 ILE D 206 42.775 25.677 −26.871 1.00 27.60 C ATOM 7851 CD1 ILE D 206 41.062 27.944 −25.123 1.00 33.24 C ATOM 7852 N SER D 207 42.124 25.263 −30.216 1.00 26.76 N ATOM 7853 CA SER D 207 42.850 24.275 −31.011 1.00 25.10 C ATOM 7854 C SER D 207 43.092 24.774 −32.421 1.00 25.42 C ATOM 7855 O SER D 207 44.051 24.369 −33.056 1.00 32.29 O ATOM 7856 CB SER D 207 42.093 22.943 −31.087 1.00 28.19 C ATOM 7857 OG SER D 207 42.052 22.281 −29.835 1.00 37.11 O ATOM 7858 N PHE D 208 42.232 25.661 −32.906 1.00 25.72 N ATOM 7859 CA PHE D 208 42.198 25.934 −34.334 1.00 26.50 C ATOM 7860 C PHE D 208 42.313 27.403 −34.734 1.00 28.53 C ATOM 7861 O PHE D 208 43.270 27.781 −35.418 1.00 35.92 O ATOM 7862 CB PHE D 208 40.955 25.294 −34.987 1.00 26.14 C ATOM 7863 CG PHE D 208 40.919 25.458 −36.477 1.00 25.37 C ATOM 7864 CD1 PHE D 208 41.694 24.653 −37.296 1.00 28.28 C ATOM 7865 CD2 PHE D 208 40.143 26.444 −37.056 1.00 24.90 C ATOM 7866 CE1 PHE D 208 41.688 24.825 −38.660 1.00 21.59 C ATOM 7867 CE2 PHE D 208 40.126 26.605 −38.411 1.00 22.80 C ATOM 7868 CZ PHE D 208 40.902 25.798 −39.215 1.00 21.99 C ATOM 7869 N TYR D 209 41.340 28.216 −34.328 1.00 29.97 N ATOM 7870 CA TYR D 209 41.245 29.609 −34.789 1.00 36.31 C ATOM 7871 C TYR D 209 42.411 30.513 −34.368 1.00 36.72 C ATOM 7872 O TYR D 209 42.888 31.320 −35.166 1.00 35.91 O ATOM 7873 CB TYR D 209 39.898 30.248 −34.397 1.00 29.81 C ATOM 7874 CG TYR D 209 38.723 29.731 −35.199 1.00 33.01 C ATOM 7875 CD1 TYR D 209 37.760 28.928 −34.611 1.00 35.42 C ATOM 7876 CD2 TYR D 209 38.586 30.029 −36.549 1.00 38.73 C ATOM 7877 CE1 TYR D 209 36.681 28.447 −35.336 1.00 30.25 C ATOM 7878 CE2 TYR D 209 37.519 29.547 −37.284 1.00 35.05 C ATOM 7879 CZ TYR D 209 36.569 28.752 −36.668 1.00 42.05 C ATOM 7880 OH TYR D 209 35.500 28.255 −37.382 1.00 45.10 O ATOM 7881 N ILE D 210 42.876 30.397 −33.130 1.00 32.26 N ATOM 7882 CA ILE D 210 44.008 31.224 −32.727 1.00 33.16 C ATOM 7883 C ILE D 210 45.298 30.819 −33.437 1.00 27.65 C ATOM 7884 O ILE D 210 45.913 31.648 −34.102 1.00 29.79 O ATOM 7885 CB ILE D 210 44.182 31.302 −31.197 1.00 30.55 C ATOM 7886 CG1 ILE D 210 43.106 32.208 −30.606 1.00 29.56 C ATOM 7887 CG2 ILE D 210 45.552 31.849 −30.829 1.00 31.81 C ATOM 7888 CD1 ILE D 210 42.862 31.973 −29.141 1.00 26.35 C ATOM 7889 N PRO D 211 45.703 29.545 −33.316 1.00 30.45 N ATOM 7890 CA PRO D 211 46.911 29.112 −34.041 1.00 29.58 C ATOM 7891 C PRO D 211 46.801 29.474 −35.518 1.00 34.65 C ATOM 7892 O PRO D 211 47.792 29.860 −36.124 1.00 39.89 O ATOM 7893 CB PRO D 211 46.905 27.589 −33.882 1.00 26.82 C ATOM 7894 CG PRO D 211 46.063 27.323 −32.687 1.00 32.49 C ATOM 7895 CD PRO D 211 45.060 28.445 −32.573 1.00 25.96 C ATOM 7896 N LEU D 212 45.602 29.362 −36.086 1.00 30.59 N ATOM 7897 CA LEU D 212 45.375 29.751 −37.479 1.00 32.12 C ATOM 7898 C LEU D 212 45.639 31.236 −37.745 1.00 34.58 C ATOM 7899 O LEU D 212 46.424 31.581 −38.629 1.00 38.10 O ATOM 7900 CB LEU D 212 43.959 29.391 −37.922 1.00 29.03 C ATOM 7901 CG LEU D 212 43.732 29.483 −39.431 1.00 27.22 C ATOM 7902 CD1 LEU D 212 44.430 28.330 −40.159 1.00 23.64 C ATOM 7903 CD2 LEU D 212 42.261 29.493 −39.731 1.00 25.17 C ATOM 7904 N LEU D 213 44.978 32.104 −36.980 1.00 34.16 N ATOM 7905 CA LEU D 213 45.169 33.546 −37.097 1.00 31.13 C ATOM 7906 C LEU D 213 46.627 33.941 −36.970 1.00 33.86 C ATOM 7907 O LEU D 213 47.092 34.856 −37.657 1.00 32.43 O ATOM 7908 CB LEU D 213 44.340 34.284 −36.059 1.00 33.64 C ATOM 7909 CG LEU D 213 42.833 34.153 −36.294 1.00 48.98 C ATOM 7910 CD1 LEU D 213 42.050 34.651 −35.095 1.00 42.89 C ATOM 7911 CD2 LEU D 213 42.415 34.887 −37.556 1.00 38.22 C ATOM 7912 N ILE D 214 47.351 33.252 −36.093 1.00 32.53 N ATOM 7913 CA ILE D 214 48.782 33.504 −35.926 1.00 36.72 C ATOM 7914 C ILE D 214 49.548 33.077 −37.169 1.00 40.01 C ATOM 7915 O ILE D 214 50.307 33.857 −37.756 1.00 41.52 O ATOM 7916 CB ILE D 214 49.361 32.739 −34.727 1.00 40.28 C ATOM 7917 CG1 ILE D 214 48.861 33.348 −33.423 1.00 29.41 C ATOM 7918 CG2 ILE D 214 50.900 32.727 −34.777 1.00 32.13 C ATOM 7919 CD1 ILE D 214 49.267 32.552 −32.239 1.00 31.92 C ATOM 7920 N MET D 215 49.336 31.831 −37.571 1.00 33.11 N ATOM 7921 CA MET D 215 50.056 31.276 −38.705 1.00 38.45 C ATOM 7922 C MET D 215 49.898 32.133 −39.957 1.00 40.90 C ATOM 7923 O MET D 215 50.846 32.301 −40.718 1.00 38.56 O ATOM 7924 CB MET D 215 49.608 29.843 −38.981 1.00 34.46 C ATOM 7925 CG MET D 215 50.381 29.181 −40.107 1.00 38.45 C ATOM 7926 SD MET D 215 49.449 27.829 −40.843 1.00 54.48 S ATOM 7927 CE MET D 215 48.159 28.764 −41.652 1.00 36.57 C ATOM 7928 N ILE D 216 48.697 32.669 −40.165 1.00 39.34 N ATOM 7929 CA ILE D 216 48.431 33.501 −41.332 1.00 37.46 C ATOM 7930 C ILE D 216 49.120 34.847 −41.221 1.00 44.19 C ATOM 7931 O ILE D 216 49.873 35.233 −42.112 1.00 47.97 O ATOM 7932 CB ILE D 216 46.929 33.718 −41.562 1.00 47.82 C ATOM 7933 CG1 ILE D 216 46.361 32.557 −42.384 1.00 41.64 C ATOM 7934 CG2 ILE D 216 46.690 35.053 −42.284 1.00 30.90 C ATOM 7935 CD1 ILE D 216 44.917 32.252 −42.080 1.00 38.28 C ATOM 7936 N PHE D 217 48.866 35.563 −40.130 1.00 37.99 N ATOM 7937 CA PHE D 217 49.508 36.848 −39.944 1.00 35.15 C ATOM 7938 C PHE D 217 51.023 36.718 −40.101 1.00 44.89 C ATOM 7939 O PHE D 217 51.668 37.596 −40.662 1.00 46.68 O ATOM 7940 CB PHE D 217 49.167 37.445 −38.584 1.00 46.62 C ATOM 7941 CG PHE D 217 49.924 38.702 −38.283 1.00 59.86 C ATOM 7942 CD1 PHE D 217 49.641 39.873 −38.964 1.00 63.34 C ATOM 7943 CD2 PHE D 217 50.938 38.708 −37.332 1.00 73.98 C ATOM 7944 CE1 PHE D 217 50.346 41.033 −38.699 1.00 80.21 C ATOM 7945 CE2 PHE D 217 51.648 39.869 −37.056 1.00 72.56 C ATOM 7946 CZ PHE D 217 51.352 41.033 −37.742 1.00 77.03 C ATOM 7947 N VAL D 218 51.590 35.615 −39.622 1.00 45.05 N ATOM 7948 CA VAL D 218 53.034 35.415 −39.716 1.00 43.64 C ATOM 7949 C VAL D 218 53.473 35.039 −41.132 1.00 41.05 C ATOM 7950 O VAL D 218 54.420 35.609 −41.668 1.00 44.65 O ATOM 7951 CB VAL D 218 53.548 34.383 −38.678 1.00 43.06 C ATOM 7952 CG1 VAL D 218 54.987 33.954 −38.995 1.00 34.70 C ATOM 7953 CG2 VAL D 218 53.463 34.966 −37.278 1.00 28.90 C ATOM 7954 N ALA D 219 52.782 34.083 −41.739 1.00 42.00 N ATOM 7955 CA ALA D 219 53.079 33.688 −43.111 1.00 39.49 C ATOM 7956 C ALA D 219 52.995 34.869 −44.074 1.00 42.38 C ATOM 7957 O ALA D 219 53.753 34.944 −45.035 1.00 44.49 O ATOM 7958 CB ALA D 219 52.143 32.577 −43.559 1.00 34.15 C ATOM 7959 N LEU D 220 52.067 35.788 −43.826 1.00 41.73 N ATOM 7960 CA LEU D 220 51.956 36.974 −44.668 1.00 43.00 C ATOM 7961 C LEU D 220 53.175 37.894 −44.534 1.00 46.18 C ATOM 7962 O LEU D 220 53.646 38.449 −45.520 1.00 45.02 O ATOM 7963 CB LEU D 220 50.650 37.726 −44.399 1.00 38.59 C ATOM 7964 CG LEU D 220 49.383 37.034 −44.936 1.00 54.14 C ATOM 7965 CD1 LEU D 220 48.220 38.012 −45.076 1.00 38.94 C ATOM 7966 CD2 LEU D 220 49.630 36.311 −46.268 1.00 26.68 C ATOM 7967 N ARG D 221 53.698 38.041 −43.326 1.00 47.95 N ATOM 7968 CA ARG D 221 54.930 38.791 −43.149 1.00 49.68 C ATOM 7969 C ARG D 221 56.055 38.110 −43.924 1.00 53.59 C ATOM 7970 O ARG D 221 56.770 38.757 −44.687 1.00 55.11 O ATOM 7971 CB ARG D 221 55.297 38.897 −41.666 1.00 43.56 C ATOM 7972 CG ARG D 221 54.333 39.707 −40.838 1.00 43.49 C ATOM 7973 CD ARG D 221 54.194 41.121 −41.359 1.00 59.36 C ATOM 7974 NE ARG D 221 53.049 41.787 −40.745 1.00 78.75 N ATOM 7975 CZ ARG D 221 52.477 42.887 −41.224 1.00 94.94 C ATOM 7976 NH1 ARG D 221 52.948 43.447 −42.331 1.00 100.40 N ATOM 7977 NH2 ARG D 221 51.433 43.424 −40.599 1.00 87.61 N ATOM 7978 N VAL D 222 56.207 36.802 −43.724 1.00 48.44 N ATOM 7979 CA VAL D 222 57.272 36.049 −44.383 1.00 45.75 C ATOM 7980 C VAL D 222 57.215 36.234 −45.896 1.00 50.10 C ATOM 7981 O VAL D 222 58.242 36.416 −46.541 1.00 57.15 O ATOM 7982 CB VAL D 222 57.218 34.549 −44.025 1.00 33.45 C ATOM 7983 CG1 VAL D 222 58.177 33.739 −44.875 1.00 27.41 C ATOM 7984 CG2 VAL D 222 57.530 34.359 −42.562 1.00 42.61 C ATOM 7985 N TYR D 223 56.009 36.192 −46.451 1.00 43.52 N ATOM 7986 CA TYR D 223 55.785 36.502 −47.860 1.00 53.84 C ATOM 7987 C TYR D 223 56.295 37.896 −48.250 1.00 59.98 C ATOM 7988 O TYR D 223 57.036 38.035 −49.210 1.00 54.81 O ATOM 7989 CB TYR D 223 54.297 36.382 −48.193 1.00 57.51 C ATOM 7990 CG TYR D 223 53.945 36.673 −49.639 1.00 76.86 C ATOM 7991 CD1 TYR D 223 54.029 35.676 −50.605 1.00 76.17 C ATOM 7992 CD2 TYR D 223 53.511 37.939 −50.035 1.00 76.34 C ATOM 7993 CE1 TYR D 223 53.702 35.928 −51.927 1.00 80.29 C ATOM 7994 CE2 TYR D 223 53.185 38.204 −51.356 1.00 75.80 C ATOM 7995 CZ TYR D 223 53.281 37.191 −52.299 1.00 93.37 C ATOM 7996 OH TYR D 223 52.956 37.439 −53.616 1.00 100.96 O ATOM 7997 N ARG D 224 55.884 38.936 −47.536 1.00 64.33 N ATOM 7998 CA ARG D 224 56.396 40.261 −47.850 1.00 64.63 C ATOM 7999 C ARG D 224 57.915 40.232 −47.801 1.00 70.13 C ATOM 8000 O ARG D 224 58.568 40.663 −48.744 1.00 68.16 O ATOM 8001 CB ARG D 224 55.858 41.321 −46.888 1.00 75.28 C ATOM 8002 CG ARG D 224 54.339 41.428 −46.869 1.00 79.04 C ATOM 8003 CD ARG D 224 53.768 41.600 −48.272 1.00 88.82 C ATOM 8004 NE ARG D 224 52.306 41.619 −48.258 1.00 89.80 N ATOM 8005 CZ ARG D 224 51.545 41.992 −49.285 1.00 90.40 C ATOM 8006 NH1 ARG D 224 52.097 42.390 −50.423 1.00 66.76 N ATOM 8007 NH2 ARG D 224 50.225 41.971 −49.172 1.00 104.25 N ATOM 8008 N GLU D 225 58.477 39.700 −46.715 1.00 65.17 N ATOM 8009 CA GLU D 225 59.930 39.699 −46.560 1.00 62.15 C ATOM 8010 C GLU D 225 60.629 38.995 −47.715 1.00 68.11 C ATOM 8011 O GLU D 225 61.614 39.498 −48.239 1.00 79.92 O ATOM 8012 CB GLU D 225 60.358 39.082 −45.229 1.00 57.07 C ATOM 8013 CG GLU D 225 60.338 40.061 −44.059 1.00 79.52 C ATOM 8014 CD GLU D 225 61.448 41.095 −44.137 1.00 86.64 C ATOM 8015 OE1 GLU D 225 62.074 41.222 −45.212 1.00 90.05 O ATOM 8016 OE2 GLU D 225 61.698 41.780 −43.120 1.00 86.69 O ATOM 8017 N ALA D 226 60.117 37.834 −48.109 1.00 63.51 N ATOM 8018 CA ALA D 226 60.671 37.097 −49.237 1.00 64.13 C ATOM 8019 C ALA D 226 60.499 37.887 −50.528 1.00 79.11 C ATOM 8020 O ALA D 226 61.297 37.761 −51.455 1.00 86.09 O ATOM 8021 CB ALA D 226 60.011 35.736 −49.360 1.00 54.87 C ATOM 8022 N LYS D 227 59.457 38.711 −50.580 1.00 76.98 N ATOM 8023 CA LYS D 227 59.164 39.513 −51.766 1.00 77.20 C ATOM 8024 C LYS D 227 60.074 40.732 −51.889 1.00 77.36 C ATOM 8025 O LYS D 227 60.899 40.807 −52.788 1.00 74.94 O ATOM 8026 CB LYS D 227 57.703 39.964 −51.754 1.00 87.99 C ATOM 8027 CG LYS D 227 57.314 40.853 −52.920 1.00 89.57 C ATOM 8028 CD LYS D 227 56.103 41.712 −52.573 1.00 90.25 C ATOM 8029 CE LYS D 227 55.693 42.584 −53.751 1.00 118.28 C ATOM 8030 NZ LYS D 227 56.826 43.411 −54.266 1.00 118.43 N ATOM 8031 N GLU D 228 59.915 41.709 −51.009 1.00 92.63 N ATOM 8032 CA GLU D 228 60.721 42.915 −51.124 1.00 85.87 C ATOM 8033 C GLU D 228 62.197 42.536 −51.171 1.00 88.02 C ATOM 8034 O GLU D 228 63.054 43.359 −51.493 1.00 96.21 O ATOM 8035 CB GLU D 228 60.423 43.883 −49.977 1.00 96.56 C ATOM 8036 CG GLU D 228 58.941 44.191 −49.778 1.00 100.69 C ATOM 8037 CD GLU D 228 58.201 44.404 −51.090 1.00 120.16 C ATOM 8038 OE1 GLU D 228 58.859 44.683 −52.120 1.00 116.52 O ATOM 8039 OE2 GLU D 228 56.955 44.292 −51.089 1.00 134.38 O ATOM 8040 N GLN D 229 62.471 41.270 −50.864 1.00 81.70 N ATOM 8041 CA GLN D 229 63.820 40.733 −50.851 1.00 85.83 C ATOM 8042 C GLN D 229 64.268 40.441 −52.268 1.00 93.42 C ATOM 8043 O GLN D 229 65.382 40.784 −52.663 1.00 114.71 O ATOM 8044 CB GLN D 229 63.822 39.426 −50.073 1.00 88.44 C ATOM 8045 CG GLN D 229 65.078 39.137 −49.299 1.00 85.28 C ATOM 8046 CD GLN D 229 65.051 37.744 −48.713 1.00 87.50 C ATOM 8047 OE1 GLN D 229 65.547 37.509 −47.608 1.00 83.56 O ATOM 8048 NE2 GLN D 229 64.454 36.806 −49.449 1.00 87.34 N ATOM 8049 N ILE D 230 63.382 39.796 −53.021 1.00 93.51 N ATOM 8050 CA ILE D 230 63.658 39.324 −54.375 1.00 95.37 C ATOM 8051 C ILE D 230 62.692 38.190 −54.638 1.00 80.95 C ATOM 8052 O ILE D 230 61.497 38.408 −54.812 1.00 91.66 O ATOM 8053 CB ILE D 230 65.087 38.771 −54.517 1.00 104.11 C ATOM 8054 CG1 ILE D 230 65.307 38.190 −55.918 1.00 99.04 C ATOM 8055 CG2 ILE D 230 65.351 37.706 −53.455 1.00 90.14 C ATOM 8056 CD1 ILE D 230 64.831 36.756 −56.073 1.00 83.25 C ATOM 8057 N ARG D 267 66.556 29.458 −54.852 1.00 95.95 N ATOM 8058 CA ARG D 267 65.724 28.261 −54.835 1.00 102.74 C ATOM 8059 C ARG D 267 65.047 28.193 −53.475 1.00 100.85 C ATOM 8060 O ARG D 267 64.219 27.317 −53.210 1.00 91.34 O ATOM 8061 CB ARG D 267 66.571 27.008 −55.052 1.00 111.25 C ATOM 8062 CG ARG D 267 67.133 26.864 −56.459 1.00 129.89 C ATOM 8063 CD ARG D 267 66.062 26.435 −57.460 1.00 130.40 C ATOM 8064 NE ARG D 267 66.618 26.229 −58.796 1.00 138.47 N ATOM 8065 CZ ARG D 267 65.936 25.752 −59.834 1.00 131.25 C ATOM 8066 NH1 ARG D 267 64.658 25.422 −59.702 1.00 116.16 N ATOM 8067 NH2 ARG D 267 66.536 25.601 −61.007 1.00 133.63 N ATOM 8068 N GLU D 268 65.424 29.133 −52.615 1.00 99.56 N ATOM 8069 CA GLU D 268 64.847 29.262 −51.287 1.00 78.15 C ATOM 8070 C GLU D 268 63.386 29.690 −51.374 1.00 73.17 C ATOM 8071 O GLU D 268 62.564 29.268 −50.565 1.00 71.46 O ATOM 8072 CB GLU D 268 65.641 30.282 −50.472 1.00 91.39 C ATOM 8073 CG GLU D 268 67.142 30.029 −50.462 1.00 119.84 C ATOM 8074 CD GLU D 268 67.529 28.835 −49.609 1.00 131.25 C ATOM 8075 OE1 GLU D 268 66.707 28.412 −48.768 1.00 132.47 O ATOM 8076 OE2 GLU D 268 68.657 28.323 −49.777 1.00 131.55 O ATOM 8077 N HIS D 269 63.068 30.526 −52.359 1.00 74.28 N ATOM 8078 CA HIS D 269 61.691 30.953 −52.578 1.00 72.83 C ATOM 8079 C HIS D 269 60.830 29.795 −53.055 1.00 57.35 C ATOM 8080 O HIS D 269 59.610 29.818 −52.919 1.00 67.94 O ATOM 8081 CB HIS D 269 61.632 32.123 −53.565 1.00 63.99 C ATOM 8082 CG HIS D 269 62.125 33.407 −52.981 1.00 88.92 C ATOM 8083 ND1 HIS D 269 61.715 34.650 −53.448 1.00 92.00 N ATOM 8084 CD2 HIS D 269 62.970 33.661 −51.960 1.00 94.74 C ATOM 8085 CE1 HIS D 269 62.305 35.592 −52.749 1.00 90.46 C ATOM 8086 NE2 HIS D 269 63.075 35.024 −51.829 1.00 92.43 N ATOM 8087 N LYS D 270 61.470 28.770 −53.595 1.00 55.39 N ATOM 8088 CA LYS D 270 60.741 27.590 −54.040 1.00 72.56 C ATOM 8089 C LYS D 270 60.438 26.669 −52.861 1.00 72.24 C ATOM 8090 O LYS D 270 59.406 25.995 −52.834 1.00 65.48 O ATOM 8091 CB LYS D 270 61.515 26.872 −55.144 1.00 73.08 C ATOM 8092 CG LYS D 270 61.745 27.776 −56.354 1.00 102.52 C ATOM 8093 CD LYS D 270 62.772 27.225 −57.332 1.00 126.84 C ATOM 8094 CE LYS D 270 63.046 28.219 −58.461 1.00 125.90 C ATOM 8095 NZ LYS D 270 61.813 28.571 −59.228 1.00 127.49 N ATOM 8096 N ALA D 271 61.333 26.664 −51.879 1.00 63.57 N ATOM 8097 CA ALA D 271 61.094 25.958 −50.630 1.00 45.39 C ATOM 8098 C ALA D 271 60.034 26.688 −49.796 1.00 55.18 C ATOM 8099 O ALA D 271 59.201 26.057 −49.137 1.00 50.07 O ATOM 8100 CB ALA D 271 62.381 25.825 −49.856 1.00 50.03 C ATOM 8101 N LEU D 272 60.069 28.018 −49.832 1.00 43.08 N ATOM 8102 CA LEU D 272 59.062 28.833 −49.166 1.00 44.91 C ATOM 8103 C LEU D 272 57.695 28.725 −49.831 1.00 47.47 C ATOM 8104 O LEU D 272 56.666 28.861 −49.171 1.00 44.87 O ATOM 8105 CB LEU D 272 59.487 30.299 −49.134 1.00 49.57 C ATOM 8106 CG LEU D 272 60.616 30.647 −48.168 1.00 47.03 C ATOM 8107 CD1 LEU D 272 60.810 32.143 −48.148 1.00 45.70 C ATOM 8108 CD2 LEU D 272 60.312 30.123 −46.777 1.00 29.86 C ATOM 8109 N LYS D 273 57.672 28.490 −51.138 1.00 57.41 N ATOM 8110 CA LYS D 273 56.397 28.428 −51.839 1.00 52.99 C ATOM 8111 C LYS D 273 55.667 27.141 −51.482 1.00 50.91 C ATOM 8112 O LYS D 273 54.438 27.095 −51.452 1.00 43.18 O ATOM 8113 CB LYS D 273 56.581 28.547 −53.349 1.00 51.54 C ATOM 8114 CG LYS D 273 55.431 29.299 −54.014 1.00 83.76 C ATOM 8115 CD LYS D 273 54.958 28.638 −55.306 1.00 81.99 C ATOM 8116 CE LYS D 273 53.869 29.471 −55.968 1.00 73.40 C ATOM 8117 NZ LYS D 273 53.316 28.808 −57.177 1.00 88.35 N ATOM 8118 N THR D 274 56.439 26.099 −51.197 1.00 51.68 N ATOM 8119 CA THR D 274 55.881 24.824 −50.775 1.00 44.79 C ATOM 8120 C THR D 274 55.340 24.914 −49.348 1.00 44.75 C ATOM 8121 O THR D 274 54.276 24.377 −49.046 1.00 41.55 O ATOM 8122 CB THR D 274 56.935 23.718 −50.858 1.00 39.54 C ATOM 8123 OG1 THR D 274 57.486 23.696 −52.179 1.00 56.89 O ATOM 8124 CG2 THR D 274 56.321 22.365 −50.553 1.00 47.87 C ATOM 8125 N LEU D 275 56.073 25.599 −48.475 1.00 41.41 N ATOM 8126 CA LEU D 275 55.604 25.819 −47.112 1.00 35.53 C ATOM 8127 C LEU D 275 54.289 26.565 −47.157 1.00 38.08 C ATOM 8128 O LEU D 275 53.365 26.233 −46.416 1.00 34.76 O ATOM 8129 CB LEU D 275 56.629 26.596 −46.287 1.00 30.71 C ATOM 8130 CG LEU D 275 57.925 25.825 −46.006 1.00 45.29 C ATOM 8131 CD1 LEU D 275 58.855 26.595 −45.055 1.00 36.74 C ATOM 8132 CD2 LEU D 275 57.619 24.419 −45.462 1.00 32.17 C ATOM 8133 N GLY D 276 54.210 27.561 −48.040 1.00 33.71 N ATOM 8134 CA GLY D 276 52.981 28.308 −48.256 1.00 34.24 C ATOM 8135 C GLY D 276 51.842 27.441 −48.771 1.00 37.00 C ATOM 8136 O GLY D 276 50.707 27.587 −48.338 1.00 32.99 O ATOM 8137 N ILE D 277 52.143 26.534 −49.696 1.00 38.32 N ATOM 8138 CA ILE D 277 51.137 25.616 −50.219 1.00 32.04 C ATOM 8139 C ILE D 277 50.618 24.686 −49.124 1.00 32.37 C ATOM 8140 O ILE D 277 49.417 24.459 −49.020 1.00 34.46 O ATOM 8141 CB ILE D 277 51.676 24.800 −51.423 1.00 36.08 C ATOM 8142 CG1 ILE D 277 51.826 25.704 −52.648 1.00 32.33 C ATOM 8143 CG2 ILE D 277 50.752 23.636 −51.768 1.00 22.56 C ATOM 8144 CD1 ILE D 277 52.909 25.266 −53.614 1.00 42.34 C ATOM 8145 N ILE D 278 51.522 24.162 −48.304 1.00 33.99 N ATOM 8146 CA ILE D 278 51.153 23.299 −47.184 1.00 32.70 C ATOM 8147 C ILE D 278 50.172 23.985 −46.216 1.00 38.70 C ATOM 8148 O ILE D 278 49.197 23.381 −45.765 1.00 31.55 O ATOM 8149 CB ILE D 278 52.405 22.848 −46.418 1.00 36.33 C ATOM 8150 CG1 ILE D 278 53.239 21.917 −47.287 1.00 52.35 C ATOM 8151 CG2 ILE D 278 52.037 22.093 −45.174 1.00 36.57 C ATOM 8152 CD1 ILE D 278 52.659 20.543 −47.390 1.00 43.55 C ATOM 8153 N MET D 279 50.432 25.254 −45.916 1.00 38.93 N ATOM 8154 CA MET D 279 49.624 26.007 −44.969 1.00 31.66 C ATOM 8155 C MET D 279 48.284 26.407 −45.558 1.00 33.52 C ATOM 8156 O MET D 279 47.277 26.446 −44.852 1.00 38.36 O ATOM 8157 CB MET D 279 50.370 27.254 −44.500 1.00 28.69 C ATOM 8158 CG MET D 279 51.667 26.967 −43.764 1.00 32.04 C ATOM 8159 SD MET D 279 52.567 28.472 −43.315 1.00 41.24 S ATOM 8160 CE MET D 279 54.030 27.745 −42.590 1.00 34.41 C ATOM 8161 N GLY D 280 48.275 26.712 −46.849 1.00 29.19 N ATOM 8162 CA GLY D 280 47.048 27.074 −47.533 1.00 28.74 C ATOM 8163 C GLY D 280 46.112 25.894 −47.692 1.00 29.40 C ATOM 8164 O GLY D 280 44.909 26.010 −47.463 1.00 30.31 O ATOM 8165 N VAL D 281 46.667 24.753 −48.085 1.00 25.84 N ATOM 8166 CA VAL D 281 45.872 23.545 −48.269 1.00 32.79 C ATOM 8167 C VAL D 281 45.304 23.051 −46.932 1.00 36.35 C ATOM 8168 O VAL D 281 44.179 22.543 −46.873 1.00 29.45 O ATOM 8169 CB VAL D 281 46.682 22.414 −48.959 1.00 31.97 C ATOM 8170 CG1 VAL D 281 45.845 21.174 −49.109 1.00 25.43 C ATOM 8171 CG2 VAL D 281 47.153 22.856 −50.322 1.00 28.74 C ATOM 8172 N PHE D 282 46.077 23.209 −45.859 1.00 28.77 N ATOM 8173 CA PHE D 282 45.590 22.839 −44.536 1.00 27.17 C ATOM 8174 C PHE D 282 44.363 23.674 −44.148 1.00 29.02 C ATOM 8175 O PHE D 282 43.364 23.148 −43.660 1.00 26.95 O ATOM 8176 CB PHE D 282 46.689 22.988 −43.490 1.00 23.81 C ATOM 8177 CG PHE D 282 46.222 22.738 −42.074 1.00 28.53 C ATOM 8178 CD1 PHE D 282 46.366 21.475 −41.491 1.00 22.01 C ATOM 8179 CD2 PHE D 282 45.647 23.767 −41.324 1.00 16.61 C ATOM 8180 CE1 PHE D 282 45.950 21.244 −40.183 1.00 19.32 C ATOM 8181 CE2 PHE D 282 45.220 23.542 −40.029 1.00 20.06 C ATOM 8182 CZ PHE D 282 45.376 22.282 −39.451 1.00 21.15 C ATOM 8183 N THR D 283 44.452 24.978 −44.370 1.00 25.35 N ATOM 8184 CA THR D 283 43.338 25.876 −44.137 1.00 24.04 C ATOM 8185 C THR D 283 42.128 25.488 −44.989 1.00 30.29 C ATOM 8186 O THR D 283 41.033 25.305 −44.472 1.00 37.88 O ATOM 8187 CB THR D 283 43.738 27.339 −44.429 1.00 26.75 C ATOM 8188 OG1 THR D 283 44.926 27.657 −43.698 1.00 26.79 O ATOM 8189 CG2 THR D 283 42.620 28.309 −44.036 1.00 26.16 C ATOM 8190 N LEU D 284 42.316 25.358 −46.293 1.00 28.75 N ATOM 8191 CA LEU D 284 41.218 24.950 −47.153 1.00 36.42 C ATOM 8192 C LEU D 284 40.555 23.637 −46.712 1.00 33.53 C ATOM 8193 O LEU D 284 39.388 23.415 −46.994 1.00 37.51 O ATOM 8194 CB LEU D 284 41.684 24.836 −48.606 1.00 43.39 C ATOM 8195 CG LEU D 284 42.164 26.138 −49.247 1.00 51.02 C ATOM 8196 CD1 LEU D 284 42.506 25.897 −50.706 1.00 44.82 C ATOM 8197 CD2 LEU D 284 41.119 27.241 −49.098 1.00 39.51 C ATOM 8198 N CYS D 285 41.287 22.768 −46.026 1.00 22.25 N ATOM 8199 CA CYS D 285 40.761 21.445 −45.722 1.00 22.27 C ATOM 8200 C CYS D 285 40.018 21.350 −44.400 1.00 30.31 C ATOM 8201 O CYS D 285 39.223 20.430 −44.206 1.00 34.61 O ATOM 8202 CB CYS D 285 41.883 20.413 −45.710 1.00 31.81 C ATOM 8203 SG CYS D 285 42.320 19.712 −47.299 1.00 38.11 S ATOM 8204 N TRP D 286 40.289 22.279 −43.485 1.00 30.28 N ATOM 8205 CA TRP D 286 39.764 22.206 −42.116 1.00 21.92 C ATOM 8206 C TRP D 286 38.831 23.356 −41.767 1.00 29.20 C ATOM 8207 O TRP D 286 37.944 23.212 −40.934 1.00 26.83 O ATOM 8208 CB TRP D 286 40.900 22.166 −41.108 1.00 18.07 C ATOM 8209 CG TRP D 286 41.431 20.802 −40.893 1.00 20.32 C ATOM 8210 CD1 TRP D 286 42.673 20.352 −41.213 1.00 17.32 C ATOM 8211 CD2 TRP D 286 40.731 19.690 −40.321 1.00 19.10 C ATOM 8212 NE1 TRP D 286 42.796 19.029 −40.872 1.00 18.62 N ATOM 8213 CE2 TRP D 286 41.618 18.598 −40.320 1.00 16.38 C ATOM 8214 CE3 TRP D 286 39.446 19.513 −39.812 1.00 16.48 C ATOM 8215 CZ2 TRP D 266 41.263 17.347 −39.829 1.00 14.33 C ATOM 8216 CZ3 TRP D 286 39.098 18.273 −39.318 1.00 20.59 C ATOM 8217 CH2 TRP D 286 40.006 17.205 −39.331 1.00 18.53 C ATOM 8218 N LEU D 287 39.037 24.503 −42.400 1.00 28.13 N ATOM 8219 CA LEU D 287 38.178 25.650 −42.156 1.00 28.72 C ATOM 8220 C LEU D 287 36.688 25.323 −42.367 1.00 30.33 C ATOM 8221 O LEU D 287 35.846 25.779 −41.601 1.00 34.00 O ATOM 8222 CB LEU D 287 38.622 26.846 −43.002 1.00 31.16 C ATOM 8223 CG LEU D 287 37.939 28.187 −42.733 1.00 37.64 C ATOM 8224 CD1 LEU D 287 37.811 28.444 −41.242 1.00 28.41 C ATOM 8225 CD2 LEU D 287 38.706 29.310 −43.402 1.00 36.84 C ATOM 8226 N PRO D 288 36.353 24.527 −43.396 1.00 32.72 N ATOM 8227 CA PRO D 288 34.920 24.212 −43.534 1.00 30.90 C ATOM 8228 C PRO D 288 34.376 23.507 −42.294 1.00 32.43 C ATOM 8229 O PRO D 288 33.370 23.935 −41.736 1.00 36.00 O ATOM 8230 CB PRO D 288 34.866 23.274 −44.753 1.00 26.84 C ATOM 8231 CG PRO D 288 36.119 23.585 −45.534 1.00 29.49 C ATOM 8232 CD PRO D 288 37.159 23.994 −44.513 1.00 31.14 C ATOM 8233 N PHE D 289 35.043 22.447 −41.856 1.00 25.46 N ATOM 8234 CA PHE D 289 34.569 21.695 −40.705 1.00 24.09 C ATOM 8235 C PHE D 289 34.424 22.533 −39.418 1.00 33.01 C ATOM 8236 O PHE D 289 33.520 22.275 −38.623 1.00 35.49 O ATOM 8237 CB PHE D 289 35.452 20.471 −40.472 1.00 22.53 C ATOM 8238 CG PHE D 289 35.278 19.841 −39.116 1.00 32.15 C ATOM 8239 CD1 PHE D 289 34.469 18.721 −38.952 1.00 32.57 C ATOM 8240 CD2 PHE D 289 35.932 20.364 −37.994 1.00 28.76 C ATOM 8241 CE1 PHE D 289 34.310 18.122 −37.697 1.00 26.39 C ATOM 8242 CE2 PHE D 289 35.780 19.774 −36.737 1.00 27.71 C ATOM 8243 CZ PHE D 289 34.972 18.648 −36.592 1.00 27.96 C ATOM 8244 N PHE D 290 35.301 23.518 −39.207 1.00 32.46 N ATOM 8245 CA PHE D 290 35.225 24.371 −38.008 1.00 31.02 C ATOM 8246 C PHE D 290 34.211 25.481 −38.179 1.00 33.73 C ATOM 8247 O PHE D 290 33.626 25.948 −37.204 1.00 33.39 O ATOM 8248 CB PHE D 290 36.590 24.954 −37.593 1.00 29.07 C ATOM 8249 CG PHE D 290 37.490 23.953 −36.917 1.00 25.36 C ATOM 8250 CD1 PHE D 290 38.493 23.309 −37.626 1.00 24.31 C ATOM 8251 CD2 PHE D 290 37.315 23.634 −35.591 1.00 25.53 C ATOM 8252 CE1 PHE D 290 39.305 22.377 −37.022 1.00 18.26 C ATOM 8253 CE2 PHE D 290 38.126 22.691 −34.984 1.00 31.45 C ATOM 8254 CZ PHE D 290 39.116 22.065 −35.702 1.00 24.13 C ATOM 8255 N LEU D 291 33.992 25.905 −39.417 1.00 30.31 N ATOM 8256 CA LEU D 291 32.937 26.878 −39.657 1.00 36.64 C ATOM 8257 C LEU D 291 31.581 26.239 −39.416 1.00 36.32 C ATOM 8258 O LEU D 291 30.689 26.851 −38.836 1.00 48.26 O ATOM 8259 CB LEU D 291 33.028 27.498 −41.050 1.00 35.77 C ATOM 8260 CG LEU D 291 34.061 28.622 −41.087 1.00 37.74 C ATOM 8261 CD1 LEU D 291 33.956 29.433 −42.365 1.00 24.96 C ATOM 8262 CD2 LEU D 291 33.859 29.511 −39.877 1.00 38.94 C ATOM 8263 N VAL D 292 31.430 24.996 −39.841 1.00 34.79 N ATOM 8264 CA VAL D 292 30.170 24.286 −39.640 1.00 37.13 C ATOM 8265 C VAL D 292 29.985 23.935 −38.164 1.00 33.65 C ATOM 8266 O VAL D 292 28.875 23.663 −37.694 1.00 35.33 O ATOM 8267 CB VAL D 292 30.086 23.046 −40.563 1.00 32.12 C ATOM 8268 CG1 VAL D 292 29.679 21.797 −39.798 1.00 30.86 C ATOM 8269 CG2 VAL D 292 29.154 23.336 −41.713 1.00 29.68 C ATOM 8270 N ASN D 293 31.089 23.978 −37.430 1.00 35.67 N ATOM 8271 CA ASN D 293 31.070 23.658 −36.010 1.00 37.64 C ATOM 8272 C ASN D 293 30.554 24.823 −35.174 1.00 34.94 C ATOM 8273 O ASN D 293 29.899 24.612 −34.172 1.00 29.15 O ATOM 8274 CB ASN D 293 32.459 23.249 −35.541 1.00 37.24 C ATOM 8275 CG ASN D 293 32.426 22.076 −34.590 1.00 46.27 C ATOM 8276 OD1 ASN D 293 31.948 20.994 −34.936 1.00 36.08 O ATOM 8277 ND2 ASN D 293 32.952 22.277 −33.386 1.00 54.55 N ATOM 8278 N ILE D 294 30.854 26.048 −35.598 1.00 39.38 N ATOM 8279 CA ILE D 294 30.354 27.233 −34.923 1.00 37.72 C ATOM 8280 C ILE D 294 28.883 27.419 −35.243 1.00 38.41 C ATOM 8281 O ILE D 294 28.120 27.961 −34.442 1.00 41.64 O ATOM 8282 CB ILE D 294 31.140 28.493 −35.337 1.00 40.31 C ATOM 8283 CG1 ILE D 294 32.580 28.381 −34.851 1.00 44.71 C ATOM 8284 CG2 ILE D 294 30.503 29.769 −34.770 1.00 29.81 C ATOM 8285 CD1 ILE D 294 33.444 29.546 −35.270 1.00 57.58 C ATOM 8286 N VAL D 295 28.482 26.952 −36.415 1.00 30.14 N ATOM 8287 CA VAL D 295 27.091 27.066 −36.826 1.00 32.81 C ATOM 8288 C VAL D 295 26.175 26.121 −36.032 1.00 36.89 C ATOM 8289 O VAL D 295 25.057 26.499 −35.691 1.00 30.26 O ATOM 8290 CB VAL D 295 26.929 26.880 −38.352 1.00 37.49 C ATOM 8291 CG1 VAL D 295 25.460 26.798 −38.748 1.00 39.69 C ATOM 8292 CG2 VAL D 295 27.612 28.012 −39.078 1.00 30.22 C ATOM 8293 N ASN D 296 26.633 24.907 −35.721 1.00 35.54 N ATOM 8294 CA ASN D 296 25.816 24.032 −34.867 1.00 40.82 C ATOM 8295 C ASN D 296 25.673 24.567 −33.462 1.00 28.01 C ATOM 8296 O ASN D 296 24.809 24.141 −32.715 1.00 27.18 O ATOM 8297 CB ASN D 296 26.319 22.584 −34.826 1.00 34.42 C ATOM 8298 CG ASN D 296 25.699 21.736 −35.921 1.00 71.75 C ATOM 8299 OD1 ASN D 296 24.503 21.424 −35.891 1.00 77.03 O ATOM 8300 ND2 ASN D 296 26.501 21.386 −36.914 1.00 76.98 N ATOM 8301 N VAL D 297 26.535 25.505 −33.110 1.00 27.97 N ATOM 8302 CA VAL D 297 26.456 26.127 −31.814 1.00 41.62 C ATOM 8303 C VAL D 297 25.262 27.088 −31.761 1.00 42.82 C ATOM 8304 O VAL D 297 24.482 27.061 −30.813 1.00 44.08 O ATOM 8305 CB VAL D 297 27.778 26.831 −31.440 1.00 43.32 C ATOM 8306 CG1 VAL D 297 27.542 27.898 −30.365 1.00 34.25 C ATOM 8307 CG2 VAL D 297 28.804 25.801 −30.967 1.00 28.85 C ATOM 8308 N PHE D 298 25.101 27.926 −32.777 1.00 37.96 N ATOM 8309 CA PHE D 298 24.000 28.880 −32.764 1.00 42.34 C ATOM 8310 C PHE D 298 22.662 28.158 −32.918 1.00 53.12 C ATOM 8311 O PHE D 298 21.693 28.441 −32.204 1.00 55.04 O ATOM 8312 CB PHE D 298 24.216 29.982 −33.810 1.00 44.58 C ATOM 8313 CG PHE D 298 25.335 30.956 −33.442 1.00 83.16 C ATOM 8314 CD1 PHE D 298 26.508 30.498 −32.832 1.00 71.03 C ATOM 8315 CD2 PHE D 298 25.217 32.320 −33.704 1.00 83.75 C ATOM 8316 CE1 PHE D 298 27.540 31.373 −32.487 1.00 51.53 C ATOM 8317 CE2 PHE D 298 26.250 33.206 −33.368 1.00 74.78 C ATOM 8318 CZ PHE D 298 27.412 32.728 −32.760 1.00 68.60 C ATOM 8319 N ASN D 299 22.633 27.185 −33.816 1.00 44.56 N ATOM 8320 CA ASN D 299 21.435 26.412 −34.057 1.00 33.98 C ATOM 8321 C ASN D 299 21.871 25.024 −34.481 1.00 36.44 C ATOM 8322 O ASN D 299 22.383 24.831 −35.585 1.00 38.36 O ATOM 8323 CB ASN D 299 20.606 27.086 −35.166 1.00 54.01 C ATOM 8324 CG ASN D 299 19.194 26.493 −35.326 1.00 62.23 C ATOM 8325 OD1 ASN D 299 18.703 25.732 −34.485 1.00 43.72 O ATOM 8326 ND2 ASN D 299 18.536 26.861 −36.421 1.00 67.04 N ATOM 8327 N ARG D 300 21.714 24.055 −33.592 1.00 42.13 N ATOM 8328 CA ARG D 300 21.758 22.670 −34.026 1.00 43.78 C ATOM 8329 C ARG D 300 20.599 22.598 −35.011 1.00 46.09 C ATOM 8330 O ARG D 300 19.808 23.537 −35.087 1.00 58.27 O ATOM 8331 CB ARG D 300 21.576 21.737 −32.831 1.00 49.64 C ATOM 8332 CG ARG D 300 22.336 22.221 −31.582 1.00 56.07 C ATOM 8333 CD ARG D 300 22.864 21.078 −30.707 1.00 78.85 C ATOM 8334 NE ARG D 300 23.808 21.543 −29.686 1.00 66.34 N ATOM 8335 CZ ARG D 300 24.109 20.870 −28.576 1.00 78.94 C ATOM 8336 NH1 ARG D 300 23.539 19.696 −28.325 1.00 72.71 N ATOM 8337 NH2 ARG D 300 24.974 21.375 −27.706 1.00 62.48 N ATOM 8338 N ASP D 301 20.496 21.530 −35.789 1.00 42.09 N ATOM 8339 CA ASP D 301 19.451 21.455 −36.836 1.00 52.98 C ATOM 8340 C ASP D 301 19.744 22.302 −38.096 1.00 45.95 C ATOM 8341 O ASP D 301 19.362 21.921 −39.201 1.00 57.49 O ATOM 8342 CB ASP D 301 18.043 21.786 −36.282 1.00 44.72 C ATOM 8343 CG ASP D 301 17.587 20.809 −35.179 1.00 60.78 C ATOM 8344 OD1 ASP D 301 17.877 19.595 −35.287 1.00 51.03 O ATOM 8345 OD2 ASP D 301 16.934 21.253 −34.200 1.00 55.47 O ATOM 8346 N LEU D 302 20.431 23.429 −37.936 1.00 46.47 N ATOM 8347 CA LEU D 302 20.655 24.352 −39.045 1.00 43.95 C ATOM 8348 C LEU D 302 21.645 23.838 −40.104 1.00 58.35 C ATOM 8349 O LEU D 302 21.998 24.563 −41.037 1.00 63.80 O ATOM 8350 CB LEU D 302 21.117 25.712 −38.513 1.00 49.78 C ATOM 8351 CG LEU D 302 20.915 26.918 −39.435 1.00 67.21 C ATOM 8352 CD1 LEU D 302 19.505 27.459 −39.293 1.00 73.77 C ATOM 8353 CD2 LEU D 302 21.927 28.011 −39.144 1.00 67.12 C ATOM 8354 N VAL D 303 22.092 22.594 −39.963 1.00 54.17 N ATOM 8355 CA VAL D 303 23.069 22.020 −40.891 1.00 47.07 C ATOM 8356 C VAL D 303 23.161 20.504 −40.726 1.00 44.79 C ATOM 8357 O VAL D 303 23.342 19.999 −39.621 1.00 48.74 O ATOM 8358 CB VAL D 303 24.463 22.697 −40.756 1.00 73.98 C ATOM 8359 CG1 VAL D 303 25.551 21.683 −40.417 1.00 52.06 C ATOM 8360 CG2 VAL D 303 24.805 23.474 −42.028 1.00 81.60 C ATOM 8361 N PRO D 304 23.027 19.783 −41.845 1.00 46.05 N ATOM 8362 CA PRO D 304 22.713 18.351 −41.960 1.00 42.69 C ATOM 8363 C PRO D 304 23.895 17.438 −41.708 1.00 47.95 C ATOM 8364 O PRO D 304 24.967 17.631 −42.284 1.00 53.21 O ATOM 8365 CB PRO D 304 22.290 18.219 −43.424 1.00 46.38 C ATOM 8366 CG PRO D 304 23.097 19.282 −44.112 1.00 46.70 C ATOM 8367 CD PRO D 304 23.051 20.442 −43.164 1.00 48.45 C ATOM 8368 N ASP D 305 23.677 16.419 −40.890 1.00 45.10 N ATOM 8369 CA ASP D 305 24.745 15.513 −40.478 1.00 50.60 C ATOM 8370 C ASP D 305 25.688 15.105 −41.619 1.00 56.72 C ATOM 8371 O ASP D 305 26.907 15.051 −41.436 1.00 58.04 O ATOM 8372 CB ASP D 305 24.154 14.284 −39.773 1.00 48.38 C ATOM 8373 CG ASP D 305 23.285 14.661 −38.563 1.00 82.04 C ATOM 8374 OD1 ASP D 305 23.789 15.350 −37.645 1.00 86.49 O ATOM 8375 OD2 ASP D 305 22.095 14.274 −38.526 1.00 78.84 O ATOM 8376 N TRP D 306 25.135 14.841 −42.799 1.00 53.90 N ATOM 8377 CA TRP D 306 25.953 14.398 −43.927 1.00 49.07 C ATOM 8378 C TRP D 306 26.995 15.448 −44.318 1.00 46.14 C ATOM 8379 O TRP D 306 28.090 15.096 −44.762 1.00 36.11 O ATOM 8380 CB TRP D 306 25.079 14.020 −45.143 1.00 39.31 C ATOM 8381 CG TRP D 306 24.470 15.208 −45.813 1.00 40.74 C ATOM 8382 CD1 TRP D 306 23.219 15.703 −45.610 1.00 39.79 C ATOM 8383 CD2 TRP D 306 25.099 16.077 −46.771 1.00 38.88 C ATOM 8384 NE1 TRP D 306 23.024 16.822 −46.387 1.00 48.43 N ATOM 8385 CE2 TRP D 306 24.164 17.074 −47.107 1.00 39.88 C ATOM 8386 CE3 TRP D 306 26.364 16.113 −47.368 1.00 48.17 C ATOM 8387 CZ2 TRP D 306 24.446 18.092 −48.023 1.00 37.91 C ATOM 8388 CZ3 TRP D 306 26.644 17.130 −48.286 1.00 48.31 C ATOM 8389 CH2 TRP D 306 25.687 18.100 −48.601 1.00 31.95 C ATOM 8390 N LEU D 307 26.648 16.729 −44.172 1.00 38.49 N ATOM 8391 CA LEU D 307 27.580 17.795 −44.510 1.00 39.42 C ATOM 8392 C LEU D 307 28.702 17.827 −43.475 1.00 45.64 C ATOM 8393 O LEU D 307 29.819 18.285 −43.738 1.00 36.32 O ATOM 8394 CB LEU D 307 26.879 19.148 −44.582 1.00 33.34 C ATOM 8395 CG LEU D 307 27.823 20.314 −44.915 1.00 38.63 C ATOM 8396 CD1 LEU D 307 28.673 20.026 −46.150 1.00 35.55 C ATOM 8397 CD2 LEU D 307 27.052 21.606 −45.101 1.00 47.66 C ATOM 8398 N PHE D 308 28.401 17.314 −42.292 1.00 44.70 N ATOM 8399 CA PHE D 308 29.391 17.255 −41.240 1.00 41.41 C ATOM 8400 C PHE D 308 30.383 16.163 −41.564 1.00 39.75 C ATOM 8401 O PHE D 308 31.590 16.348 −41.445 1.00 42.97 O ATOM 8402 CB PHE D 308 28.728 16.970 −39.902 1.00 38.18 C ATOM 8403 CG PHE D 308 29.013 18.006 −38.881 1.00 43.65 C ATOM 8404 CD1 PHE D 308 27.987 18.730 −38.303 1.00 47.48 C ATOM 8405 CD2 PHE D 308 30.318 18.295 −38.525 1.00 55.24 C ATOM 8406 CE1 PHE D 308 28.261 19.704 −37.364 1.00 45.97 C ATOM 8407 CE2 PHE D 308 30.597 19.273 −37.585 1.00 55.35 C ATOM 8408 CZ PHE D 308 29.566 19.980 −37.005 1.00 46.28 C ATOM 8409 N VAL D 309 29.867 15.018 −41.978 1.00 35.58 N ATOM 8410 CA VAL D 309 30.725 13.900 −42.287 1.00 28.15 C ATOM 8411 C VAL D 309 31.634 14.283 −43.436 1.00 32.48 C ATOM 8412 O VAL D 309 32.825 13.989 −43.412 1.00 33.33 O ATOM 8413 CB VAL D 309 29.917 12.638 −42.644 1.00 35.83 C ATOM 8414 CG1 VAL D 309 30.810 11.608 −43.288 1.00 32.75 C ATOM 8415 CG2 VAL D 309 29.272 12.053 −41.402 1.00 33.77 C ATOM 8416 N ALA D 310 31.082 14.963 −44.435 1.00 31.15 N ATOM 8417 CA ALA D 310 31.865 15.312 −45.622 1.00 34.56 C ATOM 8418 C ALA D 310 32.997 16.263 −45.270 1.00 30.94 C ATOM 8419 O ALA D 310 34.155 15.996 −45.586 1.00 26.65 O ATOM 8420 CB ALA D 310 30.986 15.911 −46.711 1.00 32.20 C ATOM 8421 N PHE D 311 32.657 17.368 −44.618 1.00 29.12 N ATOM 8422 CA PHE D 311 33.668 18.327 −44.194 1.00 30.86 C ATOM 8423 C PHE D 311 34.729 17.725 −43.278 1.00 23.35 C ATOM 8424 O PHE D 311 35.905 18.089 −43.358 1.00 20.32 O ATOM 8425 CB PHE D 311 33.028 19.552 −43.551 1.00 28.21 C ATOM 8426 CG PHE D 311 32.433 20.502 −44.543 1.00 32.17 C ATOM 8427 CD1 PHE D 311 31.477 21.426 −44.159 1.00 37.11 C ATOM 8428 CD2 PHE D 311 32.817 20.457 −45.869 1.00 29.14 C ATOM 8429 CE1 PHE D 311 30.935 22.300 −45.077 1.00 39.00 C ATOM 8430 CE2 PHE D 311 32.278 21.330 −46.784 1.00 31.00 C ATOM 8431 CZ PHE D 311 31.339 22.252 −46.393 1.00 25.18 C ATOM 8432 N ASN D 312 34.320 16.800 −42.419 1.00 21.90 N ATOM 8433 CA ASN D 312 35.272 16.112 −41.552 1.00 29.98 C ATOM 8434 C ASN D 312 36.253 15.220 −42.324 1.00 26.01 C ATOM 8435 O ASN D 312 37.406 15.082 −41.938 1.00 24.26 O ATOM 8436 CB ASN D 312 34.549 15.300 −40.471 1.00 24.35 C ATOM 8437 CG ASN D 312 35.385 15.125 −39.212 1.00 26.41 C ATOM 8438 OD1 ASN D 312 34.886 14.680 −38.181 1.00 30.82 O ATOM 8439 ND2 ASN D 312 36.661 15.488 −39.288 1.00 33.26 N ATOM 8440 N TRP D 313 35.790 14.621 −43.415 1.00 25.36 N ATOM 8441 CA TRP D 313 36.652 13.783 −44.224 1.00 22.66 C ATOM 8442 C TRP D 313 37.504 14.617 −45.152 1.00 22.05 C ATOM 8443 O TRP D 313 38.587 14.194 −45.550 1.00 25.44 O ATOM 8444 CB TRP D 313 35.847 12.731 −44.992 1.00 30.28 C ATOM 8445 CG TRP D 313 35.433 11.628 −44.079 1.00 40.01 C ATOM 8446 CD1 TRP D 313 34.330 11.608 −43.275 1.00 35.32 C ATOM 8447 CD2 TRP D 313 36.140 10.409 −43.820 1.00 36.48 C ATOM 8448 NE1 TRP D 313 34.293 10.444 −42.547 1.00 39.15 N ATOM 8449 CE2 TRP D 313 35.392 9.688 −42.858 1.00 38.86 C ATOM 8450 CE3 TRP D 313 37.320 9.849 −44.317 1.00 31.79 C ATOM 8451 CZ2 TRP D 313 35.786 8.434 −42.377 1.00 33.81 C ATOM 8452 CZ3 TRP D 313 37.713 8.603 −43.838 1.00 44.97 C ATOM 8453 CH2 TRP D 313 36.944 7.909 −42.873 1.00 35.86 C ATOM 8454 N LEU D 314 37.021 15.807 −45.489 1.00 14.95 N ATOM 8455 CA LEU D 314 37.822 16.728 −46.257 1.00 17.22 C ATOM 8456 C LEU D 314 39.109 17.017 −45.484 1.00 31.64 C ATOM 8457 O LEU D 314 40.212 16.950 −46.036 1.00 30.51 O ATOM 8458 CB LEU D 314 37.062 18.020 −46.517 1.00 19.32 C ATOM 8459 CG LEU D 314 37.975 19.085 −47.128 1.00 27.03 C ATOM 8460 CD1 LEU D 314 38.663 18.549 −48.387 1.00 17.77 C ATOM 8461 CD2 LEU D 314 37.219 20.372 −47.406 1.00 23.34 C ATOM 8462 N GLY D 315 38.958 17.329 −44.198 1.00 24.81 N ATOM 8463 CA GLY D 315 40.087 17.510 −43.301 1.00 24.03 C ATOM 8464 C GLY D 315 40.976 16.294 −43.073 1.00 23.21 C ATOM 8465 O GLY D 315 42.188 16.435 −42.954 1.00 20.76 O ATOM 8466 N TYR D 316 40.401 15.100 −42.991 1.00 21.10 N ATOM 8467 CA TYR D 316 41.246 13.919 −42.908 1.00 21.00 C ATOM 8468 C TYR D 316 42.065 13.792 −44.182 1.00 27.01 C ATOM 8469 O TYR D 316 43.242 13.446 −44.136 1.00 29.10 O ATOM 8470 CB TYR D 316 40.452 12.631 −42.721 1.00 25.78 C ATOM 8471 CG TYR D 316 39.775 12.435 −41.386 1.00 26.95 C ATOM 8472 CD1 TYR D 316 38.600 11.697 −41.308 1.00 25.65 C ATOM 8473 CD2 TYR D 316 40.299 12.980 −40.205 1.00 26.58 C ATOM 8474 CE1 TYR D 316 37.958 11.500 −40.106 1.00 32.38 C ATOM 8475 CE2 TYR D 316 39.656 12.783 −38.972 1.00 26.12 C ATOM 8476 CZ TYR D 316 38.476 12.042 −38.947 1.00 32.51 C ATOM 8477 OH TYR D 316 37.785 11.816 −37.791 1.00 25.19 O ATOM 8478 N ALA D 317 41.447 14.058 −45.329 1.00 27.93 N ATOM 8479 CA ALA D 317 42.149 13.849 −46.602 1.00 33.59 C ATOM 8480 C ALA D 317 43.411 14.707 −46.661 1.00 34.47 C ATOM 8481 O ALA D 317 44.369 14.372 −47.369 1.00 38.19 O ATOM 8482 CB ALA D 317 41.233 14.104 −47.807 1.00 24.37 C ATOM 8483 N ASN D 318 43.410 15.799 −45.897 1.00 25.75 N ATOM 8484 CA ASN D 318 44.586 16.647 −45.764 1.00 28.48 C ATOM 8485 C ASN D 318 45.856 15.889 −45.381 1.00 30.29 C ATOM 8486 O ASN D 318 46.942 16.268 −45.806 1.00 39.20 O ATOM 8487 CB ASN D 318 44.331 17.763 −44.757 1.00 29.33 C ATOM 8488 CG ASN D 318 45.504 18.716 −44.622 1.00 26.60 C ATOM 8489 OD1 ASN D 318 45.559 19.738 −45.293 1.00 36.52 O ATOM 8490 ND2 ASN D 318 46.446 18.386 −43.750 1.00 28.73 N ATOM 8491 N SER D 319 45.730 14.828 −44.587 1.00 23.22 N ATOM 8492 CA SER D 319 46.899 14.029 −44.187 1.00 26.95 C ATOM 8493 C SER D 319 47.579 13.314 −45.360 1.00 34.07 C ATOM 8494 O SER D 319 48.720 12.864 −45.244 1.00 31.33 O ATOM 8495 CB SER D 319 46.532 12.992 −43.121 1.00 27.35 C ATOM 8496 OG SER D 319 46.196 13.600 −41.883 1.00 25.20 O ATOM 8497 N ALA D 320 46.875 13.209 −46.486 1.00 37.70 N ATOM 8498 CA ALA D 320 47.407 12.543 −47.674 1.00 32.84 C ATOM 8499 C ALA D 320 48.026 13.525 −48.684 1.00 35.46 C ATOM 8500 O ALA D 320 48.820 13.128 −49.526 1.00 36.55 O ATOM 8501 CB ALA D 320 46.331 11.705 −48.328 1.00 24.83 C ATOM 8502 N MET D 321 47.681 14.803 −48.580 1.00 29.25 N ATOM 8503 CA MET D 321 48.205 15.818 −49.492 1.00 36.01 C ATOM 8504 C MET D 321 49.678 16.201 −49.355 1.00 36.05 C ATOM 8505 O MET D 321 50.347 16.432 −50.355 1.00 42.66 O ATOM 8506 CB MET D 321 47.368 17.087 −49.388 1.00 41.36 C ATOM 8507 CG MET D 321 46.013 16.951 −50.018 1.00 44.06 C ATOM 8508 SD MET D 321 44.881 18.173 −49.371 1.00 55.32 S ATOM 8509 CE MET D 321 43.370 17.678 −50.208 1.00 44.30 C ATOM 8510 N ASN D 322 50.181 16.306 −48.132 1.00 37.31 N ATOM 8511 CA ASN D 322 51.528 16.831 −47.930 1.00 36.72 C ATOM 8512 C ASN D 322 52.633 16.143 −48.742 1.00 41.76 C ATOM 8513 O ASN D 322 53.401 16.821 −49.428 1.00 44.82 O ATOM 8514 CB ASN D 322 51.888 16.897 −46.444 1.00 47.41 C ATOM 8515 CG ASN D 322 51.290 18.111 −45.751 1.00 40.90 C ATOM 8516 OD1 ASN D 322 50.105 18.392 −45.883 1.00 48.11 O ATOM 8517 ND2 ASN D 322 52.113 18.833 −45.005 1.00 37.79 N ATOM 8518 N PRO D 323 52.718 14.801 −48.680 1.00 44.70 N ATOM 8519 CA PRO D 323 53.776 14.102 −49.432 1.00 43.47 C ATOM 8520 C PRO D 323 53.715 14.417 −50.932 1.00 41.57 C ATOM 8521 O PRO D 323 54.733 14.704 −51.556 1.00 40.98 O ATOM 8522 CB PRO D 323 53.476 12.616 −49.177 1.00 37.92 C ATOM 8523 CG PRO D 323 52.639 12.589 −47.940 1.00 44.64 C ATOM 8524 CD PRO D 323 51.831 13.862 −47.968 1.00 48.51 C ATOM 8525 N ILE D 324 52.518 14.366 −51.499 1.00 32.52 N ATOM 8526 CA ILE D 324 52.324 14.815 −52.863 1.00 39.17 C ATOM 8527 C ILE D 324 52.959 16.196 −53.073 1.00 36.15 C ATOM 8528 O ILE D 324 53.822 16.357 −53.926 1.00 42.86 O ATOM 8529 CB ILE D 324 50.819 14.823 −53.244 1.00 40.12 C ATOM 8530 CG1 ILE D 324 50.333 13.390 −53.484 1.00 28.43 C ATOM 8531 CG2 ILE D 324 50.570 15.697 −54.472 1.00 32.13 C ATOM 8532 CD1 ILE D 324 48.822 13.239 −53.498 1.00 40.00 C ATOM 8533 N ILE D 325 52.544 17.185 −52.291 1.00 32.27 N ATOM 8534 CA ILE D 325 53.085 18.536 −52.429 1.00 44.78 C ATOM 8535 C ILE D 325 54.631 18.612 −52.384 1.00 48.42 C ATOM 8536 O ILE D 325 55.231 19.468 −53.043 1.00 36.31 O ATOM 8537 CB ILE D 325 52.468 19.478 −51.372 1.00 37.76 C ATOM 8538 CG1 ILE D 325 50.957 19.528 −51.541 1.00 30.30 C ATOM 8539 CG2 ILE D 325 53.064 20.885 −51.456 1.00 40.79 C ATOM 8540 CD1 ILE D 325 50.240 20.226 −50.399 1.00 32.30 C ATOM 8541 N TYR D 326 55.268 17.728 −51.612 1.00 34.91 N ATOM 8542 CA TYR D 326 56.720 17.746 −51.473 1.00 39.36 C ATOM 8543 C TYR D 326 57.424 17.249 −52.724 1.00 53.06 C ATOM 8544 O TYR D 326 58.646 17.356 −52.851 1.00 49.24 O ATOM 8545 CB TYR D 326 57.183 16.871 −50.316 1.00 50.03 C ATOM 8546 CG TYR D 326 56.708 17.304 −48.960 1.00 48.46 C ATOM 8547 CD1 TYR D 326 56.427 16.360 −47.977 1.00 45.38 C ATOM 8548 CD2 TYR D 326 56.538 18.646 −48.656 1.00 48.02 C ATOM 8549 CE1 TYR D 326 55.995 16.738 −46.734 1.00 38.79 C ATOM 8550 CE2 TYR D 326 56.097 19.037 −47.406 1.00 44.34 C ATOM 8551 CZ TYR D 326 55.826 18.075 −46.452 1.00 41.61 C ATOM 8552 OH TYR D 326 55.378 18.444 −45.210 1.00 44.51 O ATOM 8553 N CYS D 327 56.661 16.669 −53.638 1.00 50.06 N ATOM 8554 CA CYS D 327 57.239 16.199 −54.883 1.00 42.80 C ATOM 8555 C CYS D 327 57.586 17.384 −55.775 1.00 51.68 C ATOM 8556 O CYS D 327 58.288 17.233 −56.769 1.00 62.06 O ATOM 8557 CB CYS D 327 56.301 15.217 −55.565 1.00 35.52 C ATOM 8558 SG CYS D 327 56.198 13.645 −54.671 1.00 58.05 S ATOM 8559 N ARG D 328 57.108 18.566 −55.387 1.00 47.54 N ATOM 8560 CA ARG D 328 57.484 19.822 −56.025 1.00 49.29 C ATOM 8561 C ARG D 328 58.977 20.076 −55.897 1.00 57.89 C ATOM 8562 O ARG D 328 59.591 20.676 −56.774 1.00 62.66 O ATOM 8563 CB ARG D 328 56.745 20.985 −55.375 1.00 49.28 C ATOM 8564 CG ARG D 328 55.276 21.091 −55.731 1.00 60.98 C ATOM 8565 CD ARG D 328 54.715 22.252 −54.962 1.00 52.06 C ATOM 8566 NE ARG D 328 55.796 23.190 −54.701 1.00 56.38 N ATOM 8567 CZ ARG D 328 55.961 24.338 −55.345 1.00 63.00 C ATOM 8568 NH1 ARG D 328 55.090 24.705 −56.275 1.00 67.31 N ATOM 8569 NH2 ARG D 328 56.984 25.128 −55.042 1.00 61.76 N ATOM 8570 N SER D 329 59.550 19.645 −54.779 1.00 65.88 N ATOM 8571 CA SER D 329 60.987 19.740 −54.578 1.00 64.23 C ATOM 8572 C SER D 329 61.676 18.622 −55.331 1.00 70.12 C ATOM 8573 O SER D 329 61.132 17.526 −55.456 1.00 65.98 O ATOM 8574 CB SER D 329 61.341 19.633 −53.098 1.00 72.32 C ATOM 8575 OG SER D 329 62.660 19.135 −52.940 1.00 66.64 O ATOM 8576 N PRO D 330 62.889 18.893 −55.826 1.00 86.13 N ATOM 8577 CA PRO D 330 63.672 17.918 −56.589 1.00 75.79 C ATOM 8578 C PRO D 330 64.286 16.871 −55.671 1.00 72.07 C ATOM 8579 O PRO D 330 64.447 15.719 −56.072 1.00 63.80 O ATOM 8580 CB PRO D 330 64.775 18.773 −57.231 1.00 77.38 C ATOM 8581 CG PRO D 330 64.386 20.222 −56.967 1.00 91.37 C ATOM 8582 CD PRO D 330 63.584 20.185 −55.712 1.00 90.21 C ATOM 8583 N ASP D 331 64.609 17.275 −54.446 1.00 78.20 N ATOM 8584 CA ASP D 331 65.266 16.400 −53.478 1.00 75.09 C ATOM 8585 C ASP D 331 64.360 15.272 −52.999 1.00 67.51 C ATOM 8586 O ASP D 331 64.754 14.110 −53.009 1.00 63.80 O ATOM 8587 CB ASP D 331 65.748 17.209 −52.274 1.00 90.05 C ATOM 8588 CG ASP D 331 66.566 18.417 −52.675 1.00 99.54 C ATOM 8589 OD1 ASP D 331 66.980 18.486 −53.850 1.00 95.72 O ATOM 8590 OD2 ASP D 331 66.795 19.295 −51.814 1.00 111.50 O ATOM 8591 N PHE D 332 63.153 15.623 −52.561 1.00 71.23 N ATOM 8592 CA PHE D 332 62.179 14.630 −52.119 1.00 69.55 C ATOM 8593 C PHE D 332 61.870 13.672 −53.261 1.00 69.17 C ATOM 8594 O PHE D 332 61.815 12.457 −53.073 1.00 62.25 O ATOM 8595 CB PHE D 332 60.885 15.301 −51.648 1.00 67.26 C ATOM 8596 CG PHE D 332 60.948 15.846 −50.244 1.00 66.82 C ATOM 8597 CD1 PHE D 332 61.197 17.195 −50.016 1.00 62.39 C ATOM 8598 CD2 PHE D 332 60.738 15.013 −49.150 1.00 66.40 C ATOM 8599 CE1 PHE D 332 61.242 17.710 −48.719 1.00 62.29 C ATOM 8600 CE2 PHE D 332 60.787 15.518 −47.845 1.00 60.47 C ATOM 8601 CZ PHE D 332 61.040 16.871 −47.633 1.00 53.48 C ATOM 8602 N ARG D 333 61.669 14.246 −54.443 1.00 71.03 N ATOM 8603 CA ARG D 333 61.389 13.500 −55.663 1.00 59.85 C ATOM 8604 C ARG D 333 62.494 12.480 −55.934 1.00 62.75 C ATOM 8605 O ARG D 333 62.228 11.281 −56.028 1.00 63.64 O ATOM 8606 CB ARG D 333 61.283 14.480 −56.827 1.00 65.60 C ATOM 8607 CG ARG D 333 60.158 14.222 −57.797 1.00 69.61 C ATOM 8608 CD ARG D 333 59.833 15.501 −58.563 1.00 77.89 C ATOM 8609 NE ARG D 333 60.998 16.384 −58.677 1.00 87.50 N ATOM 8610 CZ ARG D 333 60.963 17.619 −59.180 1.00 85.86 C ATOM 8611 NH1 ARG D 333 59.820 18.124 −59.624 1.00 82.44 N ATOM 8612 NH2 ARG D 333 62.072 18.351 −59.240 1.00 64.36 N ATOM 8613 N LYS D 334 63.730 12.963 −56.063 1.00 63.75 N ATOM 8614 CA LYS D 334 64.899 12.092 −56.221 1.00 71.16 C ATOM 8615 C LYS D 334 64.877 10.979 −55.181 1.00 70.64 C ATOM 8616 O LYS D 334 65.039 9.801 −55.504 1.00 62.05 O ATOM 8617 CB LYS D 334 66.209 12.881 −56.039 1.00 87.21 C ATOM 8618 CG LYS D 334 66.565 13.908 −57.123 1.00 87.99 C ATOM 8619 CD LYS D 334 67.948 14.519 −56.833 1.00 88.69 C ATOM 8620 CE LYS D 334 68.087 15.949 −57.355 1.00 88.99 C ATOM 8621 NZ LYS D 334 69.167 16.716 −56.646 1.00 63.98 N ATOM 8622 N ALA D 335 64.686 11.378 −53.926 1.00 73.95 N ATOM 8623 CA ALA D 335 64.730 10.468 −52.782 1.00 71.55 C ATOM 8624 C ALA D 335 63.564 9.485 −52.741 1.00 67.66 C ATOM 8625 O ALA D 335 63.741 8.333 −52.358 1.00 60.79 O ATOM 8626 CB ALA D 335 64.801 11.256 −51.482 1.00 70.69 C ATOM 8627 N PHE D 336 62.373 9.946 −53.117 1.00 70.79 N ATOM 8628 CA PHE D 336 61.218 9.063 −53.219 1.00 72.39 C ATOM 8629 C PHE D 336 61.501 7.964 −54.248 1.00 78.71 C ATOM 8630 O PHE D 336 61.080 6.821 −54.081 1.00 78.71 O ATOM 8631 CB PHE D 336 59.952 9.830 −53.631 1.00 70.56 C ATOM 8632 CG PHE D 336 59.462 10.826 −52.606 1.00 75.48 C ATOM 8633 CD1 PHE D 336 59.528 10.548 −51.248 1.00 76.03 C ATOM 8634 CD2 PHE D 336 58.894 12.031 −53.011 1.00 73.48 C ATOM 8635 CE1 PHE D 336 59.063 11.466 −50.308 1.00 63.21 C ATOM 8636 CE2 PHE D 336 58.431 12.951 −52.080 1.00 69.06 C ATOM 8637 CZ PHE D 336 58.519 12.667 −50.725 1.00 62.63 C ATOM 8638 N LYS D 337 62.219 8.319 −55.311 1.00 79.93 N ATOM 8639 CA LYS D 337 62.511 7.376 −56.388 1.00 81.12 C ATOM 8640 C LYS D 337 63.625 6.389 −56.021 1.00 76.84 C ATOM 8641 O LYS D 337 63.493 5.189 −56.265 1.00 76.58 O ATOM 8642 CB LYS D 337 62.823 8.115 −57.696 1.00 80.16 C ATOM 8643 CG LYS D 337 61.691 9.024 −58.164 1.00 82.54 C ATOM 8644 CD LYS D 337 61.806 9.380 −59.647 1.00 89.62 C ATOM 8645 CE LYS D 337 60.631 10.249 −60.100 1.00 91.61 C ATOM 8646 NZ LYS D 337 60.651 10.553 −61.560 1.00 82.56 N ATOM 8647 N ARG D 338 64.716 6.886 −55.443 1.00 71.06 N ATOM 8648 CA ARG D 338 65.725 5.996 −54.874 1.00 83.59 C ATOM 8649 C ARG D 338 65.011 4.946 −54.030 1.00 83.42 C ATOM 8650 O ARG D 338 65.141 3.746 −54.261 1.00 82.98 O ATOM 8651 CB ARG D 338 66.694 6.757 −53.966 1.00 88.62 C ATOM 8652 CG ARG D 338 67.496 7.868 −54.616 1.00 98.18 C ATOM 8653 CD ARG D 338 68.417 8.503 −53.573 1.00 106.87 C ATOM 8654 NE ARG D 338 69.483 9.302 −54.172 1.00 135.96 N ATOM 8655 CZ ARG D 338 70.563 9.724 −53.518 1.00 134.03 C ATOM 8656 NH1 ARG D 338 70.731 9.422 −52.236 1.00 125.41 N ATOM 8657 NH2 ARG D 338 71.480 10.448 −54.149 1.00 114.84 N ATOM 8658 N LEU D 339 64.246 5.428 −53.053 1.00 88.95 N ATOM 8659 CA LEU D 339 63.517 4.583 −52.106 1.00 87.86 C ATOM 8660 C LEU D 339 62.587 3.562 −52.764 1.00 88.81 C ATOM 8661 O LEU D 339 62.336 2.491 −52.207 1.00 83.89 O ATOM 8662 CB LEU D 339 62.692 5.456 −51.157 1.00 83.67 C ATOM 8663 CG LEU D 339 63.398 6.362 −50.147 1.00 89.49 C ATOM 8664 CD1 LEU D 339 62.417 7.408 −49.632 1.00 82.25 C ATOM 8665 CD2 LEU D 339 63.991 5.556 −48.995 1.00 73.40 C ATOM 8666 N LEU D 340 62.057 3.898 −53.934 1.00 86.32 N ATOM 8667 CA LEU D 340 61.143 3.000 −54.628 1.00 88.02 C ATOM 8668 C LEU D 340 61.871 2.158 −55.685 1.00 85.87 C ATOM 8669 O LEU D 340 61.337 1.884 −56.760 1.00 84.19 O ATOM 8670 CB LEU D 340 59.980 3.793 −55.234 1.00 85.39 C ATOM 8671 CG LEU D 340 59.036 4.429 −54.202 1.00 82.90 C ATOM 8672 CD1 LEU D 340 58.348 5.686 −54.736 1.00 78.73 C ATOM 8673 CD2 LEU D 340 58.012 3.412 −53.711 1.00 72.18 C ATOM 8674 C16 PDL D 400 34.229 20.502 −31.029 1.00 37.57 C ATOM 8675 N3 PDL D 400 33.164 20.648 −30.675 1.00 46.59 N ATOM 8676 N1 PDL D 400 36.770 20.970 −30.897 1.00 37.28 N ATOM 8677 C1 PDL D 400 35.570 20.327 −31.476 1.00 28.68 C ATOM 8678 C2 PDL D 400 36.018 19.415 −32.613 1.00 28.59 C ATOM 8679 C3 PDL D 400 37.484 19.555 −32.704 1.00 30.84 C ATOM 8680 C4 PDL D 400 38.459 18.903 −33.655 1.00 24.90 C ATOM 8681 C5 PDL D 400 39.941 19.197 −33.553 1.00 30.73 C ATOM 8682 C6 PDL D 400 40.443 20.161 −32.480 1.00 34.53 C ATOM 8683 C7 PDL D 400 39.462 20.833 −31.522 1.00 31.87 C ATOM 8684 C8 PDL D 400 37.961 20.523 −31.636 1.00 33.85 C ATOM 8685 O1 PDL D 400 37.965 18.058 −34.646 1.00 35.43 O ATOM 8686 C9 PDL D 400 38.363 16.721 −34.734 1.00 37.29 C ATOM 8687 C10 PDL D 400 37.404 16.098 −35.744 1.00 32.42 C ATOM 8688 O2 PDL D 400 38.137 15.290 −36.630 1.00 27.86 O ATOM 8689 C11 PDL D 400 36.335 15.315 −34.963 1.00 22.61 C ATOM 8690 N2 PDL D 400 35.771 14.176 −35.692 1.00 39.48 N ATOM 8691 C12 PDL D 400 34.935 13.380 −34.777 1.00 41.45 C ATOM 8692 C13 PDL D 400 33.676 14.227 −34.453 1.00 20.04 C ATOM 8693 C14 PDL D 400 35.727 13.042 −33.480 1.00 24.70 C ATOM 8694 C15 PDL D 400 34.541 12.053 −35.475 1.00 28.56 C ATOM 8695 NA NA D 401 28.626 6.588 −26.566 1.00 43.36 Na ATOM 8696 C1 8TG 500 10.993 30.178 7.889 1.00 37.04 C ATOM 8697 S1 8TG 500 9.765 29.130 8.728 1.00 44.60 S ATOM 8698 C2 8TG 500 11.138 29.728 6.402 1.00 37.52 C ATOM 8699 O2 8TG 500 11.795 28.486 6.285 1.00 34.58 O ATOM 8700 C3 8TG 500 11.825 30.766 5.489 1.00 34.16 C ATOM 8701 O3 8TG 500 11.470 30.384 4.183 1.00 38.38 O ATOM 8702 C4 8TG 500 11.275 32.160 5.791 1.00 35.70 C ATOM 8703 O4 8TG 500 12.019 33.168 5.170 1.00 50.67 O ATOM 8704 C5 8TG 500 11.306 32.464 7.279 1.00 44.51 C ATOM 8705 O5 8TG 500 10.500 31.537 8.035 1.00 42.28 O ATOM 8706 C6 8TG 500 10.790 33.889 7.463 1.00 45.31 C ATOM 8707 O6 8TG 500 9.389 33.845 7.426 1.00 47.54 O ATOM 8708 C1′ 8TG 500 9.666 29.823 10.414 1.00 41.86 C ATOM 8709 C2′ 8TG 500 11.085 29.848 11.032 1.00 37.52 C ATOM 8710 C3′ 8TG 500 11.126 28.808 12.177 1.00 39.74 C ATOM 8711 C4′ 8TG 500 12.544 28.220 12.368 1.00 33.61 C ATOM 8712 C5′ 8TG 500 13.597 29.354 12.407 1.00 35.15 C ATOM 8713 C6′ 8TG 500 14.980 28.671 12.503 1.00 45.87 C ATOM 8714 C7′ 8TG 500 15.968 29.365 11.540 1.00 39.33 C ATOM 8715 C8′ 8TG 500 17.398 28.888 11.867 1.00 43.93 C ATOM 8716 C1 8TG 501 32.608 19.475 11.900 1.00 90.15 C ATOM 8717 S1 8TG 501 31.628 17.960 11.587 1.00 93.54 S ATOM 8718 C2 8TG 501 33.626 19.696 10.750 1.00 104.82 C ATOM 8719 O2 8TG 501 34.302 18.505 10.395 1.00 77.91 O ATOM 8720 C3 8TG 501 34.557 20.858 11.161 1.00 115.79 C ATOM 8721 O3 8TG 501 35.467 21.085 10.115 1.00 104.95 O ATOM 8722 C4 8TG 501 33.692 22.112 11.340 1.00 120.59 C ATOM 8723 O4 8TG 501 34.439 23.174 11.887 1.00 114.75 O ATOM 8724 C5 8TG 501 32.447 21.890 12.218 1.00 122.15 C ATOM 8725 O5 8TG 501 31.738 20.638 12.008 1.00 120.40 O ATOM 8726 C6 8TG 501 31.501 23.099 12.065 1.00 109.10 C ATOM 8727 O6 8TG 501 30.488 23.093 13.037 1.00 82.15 O ATOM 8728 C1′ 8TG 501 30.222 18.330 10.469 1.00 53.70 C ATOM 8729 C2′ 8TG 501 29.563 16.996 10.048 1.00 39.87 C ATOM 8730 C3′ 8TG 501 28.320 16.751 10.935 1.00 34.30 C ATOM 8731 C4′ 8TG 501 27.208 16.163 10.052 1.00 22.54 C ATOM 8732 C5′ 8TG 501 26.674 14.878 10.731 1.00 16.34 C ATOM 8733 C6′ 8TG 501 25.235 14.679 10.209 1.00 18.79 C ATOM 8734 C7′ 8TG 501 25.041 13.222 9.743 1.00 26.21 C ATOM 8735 C8′ 8TG 501 23.603 13.076 9.237 1.00 18.47 C ATOM 8736 C1 8TG 502 31.062 22.948 −17.988 1.00 63.93 C ATOM 8737 S1 8TG 502 31.491 24.487 −18.897 1.00 88.98 S ATOM 8738 C2 8TG 502 29.787 22.257 −18.566 1.00 72.41 C ATOM 8739 O2 8TG 502 28.709 23.169 −18.623 1.00 77.66 O ATOM 8740 C3 8TG 502 29.445 20.982 −17.747 1.00 68.42 C ATOM 8741 O3 8TG 502 28.305 20.342 −18.288 1.00 51.95 O ATOM 8742 C4 8TG 502 30.667 20.050 −17.795 1.00 55.05 C ATOM 8743 O4 8TG 502 30.474 18.850 −17.077 1.00 41.32 O ATOM 8744 C5 8TG 502 31.968 20.754 −17.349 1.00 56.59 C ATOM 8745 O5 8TG 502 32.214 22.054 −17.951 1.00 56.64 O ATOM 8746 C6 8TG 502 32.105 20.825 −15.807 1.00 75.21 C ATOM 8747 O6 8TG 502 33.129 21.699 −15.377 1.00 60.34 O ATOM 8748 C1′ 8TG 502 33.304 24.586 −19.169 1.00 42.60 C ATOM 8749 C2′ 8TG 502 33.686 23.994 −20.546 1.00 27.43 C ATOM 8750 C3′ 8TG 502 35.148 23.481 −20.495 1.00 30.02 C ATOM 8751 C4′ 8TG 502 36.133 24.513 −21.102 1.00 32.30 C ATOM 8752 C5′ 8TG 502 36.762 23.924 −22.397 1.00 35.98 C ATOM 8753 C6′ 8TG 502 38.306 24.074 −22.368 1.00 32.25 C ATOM 8754 C7′ 8TG 502 38.901 23.416 −23.643 1.00 27.76 C ATOM 8755 C8′ 8TG 502 40.179 24.166 −24.074 1.00 27.49 C ATOM 8756 C1 8TG 503 38.078 7.692 −18.116 1.00 34.01 C ATOM 8757 S1 8TG 503 37.381 8.321 −19.659 1.00 48.31 S ATOM 8758 C2 8TG 503 38.737 6.287 −18.184 1.00 32.37 C ATOM 8759 O2 8TG 503 37.807 5.367 −18.721 1.00 38.95 O ATOM 8760 C3 8TG 503 39.064 5.877 −16.731 1.00 33.15 C ATOM 8761 O3 8TG 503 39.978 4.818 −16.777 1.00 53.58 O ATOM 8762 C4 8TG 503 39.729 7.001 −15.940 1.00 32.23 C ATOM 8763 O4 8TG 503 39.631 6.718 −14.569 1.00 65.01 O ATOM 8764 C5 8TG 503 39.186 8.411 −16.195 1.00 36.99 C ATOM 8765 O5 8TG 503 38.948 8.702 −17.586 1.00 32.95 O ATOM 8766 C6 8TG 503 40.181 9.470 −15.738 1.00 47.42 C ATOM 8767 O6 8TG 503 40.173 10.410 −16.778 1.00 37.05 O ATOM 8768 C1′ 8TG 503 38.121 9.963 −19.919 1.00 36.29 C ATOM 8769 C2′ 8TG 503 38.495 10.094 −21.418 1.00 51.31 C ATOM 8770 C3′ 8TG 503 39.174 8.801 −21.946 1.00 29.03 C ATOM 8771 C4′ 8TG 503 39.815 9.077 −23.330 1.00 27.01 C ATOM 8772 C5′ 8TG 503 41.159 9.842 −23.184 1.00 24.46 C ATOM 8773 C6′ 8TG 503 42.327 8.909 −22.767 1.00 27.21 C ATOM 8774 C7′ 8TG 503 43.657 9.561 −23.229 1.00 48.34 C ATOM 8775 C8′ 8TG 503 44.820 9.277 −22.259 1.00 28.64 C ATOM 8776 C1 8TG 504 23.266 27.271 −22.442 1.00 106.91 C ATOM 8777 S1 8TG 504 24.230 28.721 −23.001 1.00 88.64 S ATOM 8778 C2 8TG 504 21.769 27.515 −22.773 1.00 116.38 C ATOM 8779 O2 8TG 504 21.344 28.799 −22.371 1.00 105.09 O ATOM 8780 C3 8TG 504 20.983 26.422 −22.037 1.00 124.77 C ATOM 8781 O3 8TG 504 19.595 26.661 −22.121 1.00 97.72 O ATOM 8782 C4 8TG 504 21.374 25.071 −22.644 1.00 125.35 C ATOM 8783 O4 8TG 504 20.732 24.920 −23.884 1.00 117.30 O ATOM 8784 C5 8TG 504 22.900 24.856 −22.811 1.00 124.17 C ATOM 8785 O5 8TG 504 23.743 26.027 −23.028 1.00 107.69 O ATOM 8786 C6 8TG 504 23.182 23.798 −23.903 1.00 114.67 C ATOM 8787 O6 8TG 504 24.551 23.473 −23.991 1.00 72.69 O ATOM 8788 C1′ 8TG 504 25.758 28.308 −23.916 1.00 30.56 C ATOM 8789 C2′ 8TG 504 26.428 29.663 −24.256 1.00 32.55 C ATOM 8790 C3′ 8TG 504 27.880 29.428 −24.741 1.00 42.76 C ATOM 8791 C4′ 8TG 504 28.874 30.473 −24.171 1.00 30.69 C ATOM 8792 C5′ 8TG 504 30.225 30.284 −24.926 1.00 42.38 C ATOM 8793 C6′ 8TG 504 31.484 30.595 −24.071 1.00 27.05 C ATOM 8794 C7′ 8TG 504 32.749 30.447 −24.958 1.00 29.84 C ATOM 8795 C8′ 8TG 504 33.956 31.242 −24.409 1.00 22.84 C ATOM 8796 C1 8TG 505 3.430 16.859 6.928 1.00 66.25 C ATOM 8797 S1 8TG 505 2.975 15.077 6.894 1.00 110.67 S ATOM 8798 C2 8TG 505 4.034 17.386 5.566 1.00 72.15 C ATOM 8799 O2 8TG 505 4.001 16.400 4.549 1.00 98.40 O ATOM 8800 C3 8TG 505 3.566 18.793 5.038 1.00 87.45 C ATOM 8801 O3 8TG 505 3.308 18.793 3.647 1.00 85.83 O ATOM 8802 C4 8TG 505 2.400 19.453 5.778 1.00 81.01 C ATOM 8803 O4 8TG 505 2.543 20.858 5.837 1.00 63.58 O ATOM 8804 C5 8TG 505 2.428 18.975 7.211 1.00 64.81 C ATOM 8805 O5 8TG 505 2.237 17.564 7.368 1.00 71.69 O ATOM 8806 C6 8TG 505 1.490 19.823 8.058 1.00 60.70 C ATOM 8807 O6 8TG 505 2.287 20.324 9.097 1.00 68.65 O ATOM 8808 C1′ 8TG 505 3.906 14.159 8.175 1.00 60.99 C ATOM 8809 C2′ 8TG 505 5.365 14.683 8.258 1.00 45.47 C ATOM 8810 C3′ 8TG 505 5.896 14.352 9.675 1.00 41.77 C ATOM 8811 C4′ 8TG 505 7.352 14.825 9.892 1.00 37.65 C ATOM 8812 C5′ 8TG 505 7.999 13.908 10.967 1.00 29.55 C ATOM 8813 C6′ 8TG 505 9.506 14.200 11.127 1.00 38.75 C ATOM 8814 C7′ 8TG 505 9.713 15.109 12.363 1.00 45.04 C ATOM 8815 C8′ 8TG 505 11.192 15.051 12.796 1.00 25.19 C ATOM 8816 C1′ 8TG 506 −2.430 10.405 12.432 1.00 27.63 C ATOM 8817 C2′ 8TG 506 −2.097 8.958 12.878 1.00 31.79 C ATOM 8818 C3′ 8TG 506 −0.758 8.868 13.664 1.00 33.40 C ATOM 8819 C4′ 8TG 506 0.430 8.460 12.756 1.00 41.94 C ATOM 8820 C5′ 8TG 506 1.611 7.945 13.632 1.00 44.21 C ATOM 8821 C6′ 8TG 506 2.984 8.042 12.905 1.00 38.42 C ATOM 8822 C7′ 8TG 506 4.126 7.789 13.928 1.00 39.56 C ATOM 8823 C8′ 8TG 506 5.513 7.582 13.276 1.00 28.31 C ATOM 8824 C1 8TG 507 28.439 3.060 41.727 1.00 86.98 C ATOM 8825 S1 8TG 507 28.607 3.947 40.129 1.00 104.80 S ATOM 8826 C2 8TG 507 29.828 2.439 42.050 1.00 87.16 C ATOM 8827 O2 8TG 507 30.146 1.485 41.068 1.00 94.81 O ATOM 8828 C3 8TG 507 29.868 1.780 43.438 1.00 83.65 C ATOM 8829 O3 8TG 507 31.201 1.444 43.718 1.00 80.40 O ATOM 8830 C4 8TG 507 29.456 2.830 44.455 1.00 102.43 C ATOM 8831 O4 8TG 507 29.460 2.255 45.739 1.00 85.58 O ATOM 8832 C5 8TG 507 28.074 3.398 44.109 1.00 107.02 C ATOM 8833 O5 8TG 507 27.982 3.964 42.776 1.00 94.18 O ATOM 8834 C6 8TG 507 27.628 4.420 45.168 1.00 99.65 C ATOM 8835 O6 8TG 507 26.229 4.532 45.157 1.00 93.29 O ATOM 8836 C1′ 8TG 507 27.143 4.985 39.754 1.00 82.08 C ATOM 8837 C2′ 8TG 507 27.499 5.991 38.628 1.00 68.13 C ATOM 8838 C3′ 8TG 507 27.289 5.372 37.223 1.00 52.73 C ATOM 8839 C4′ 8TG 507 26.044 6.020 36.579 1.00 38.44 C ATOM 8840 C5′ 8TG 507 26.270 6.213 35.063 1.00 39.71 C ATOM 8841 C6′ 8TG 507 27.146 7.465 34.838 1.00 51.90 C ATOM 8842 C7′ 8TG 507 28.020 7.272 33.581 1.00 36.63 C ATOM 8843 C8′ 8TG 507 27.150 6.726 32.430 1.00 60.74 C ATOM 8844 C1 DMU 510 62.736 16.453 −22.348 1.00 116.44 C ATOM 8845 C10 DMU 510 66.802 15.892 −20.286 1.00 141.54 C ATOM 8846 C11 DMU 510 69.835 17.900 −21.184 1.00 116.62 C ATOM 8847 C18 DMU 510 60.720 19.342 −22.513 1.00 68.47 C ATOM 8848 C19 DMU 510 59.249 19.715 −22.750 1.00 44.14 C ATOM 8849 C2 DMU 510 63.836 15.811 −21.476 1.00 130.58 C ATOM 8850 C22 DMU 510 58.684 20.283 −21.432 1.00 44.98 C ATOM 8851 C25 DMU 510 57.148 20.435 −21.479 1.00 35.88 C ATOM 8852 C28 DMU 510 56.772 21.801 −20.872 1.00 29.61 C ATOM 8853 C3 DMU 510 64.672 16.872 −20.718 1.00 137.39 C ATOM 8854 C31 DMU 510 55.791 22.583 −21.768 1.00 23.05 C ATOM 8855 C34 DMU 510 54.389 22.609 −21.127 1.00 19.25 C ATOM 8856 C37 DMU 510 53.753 24.004 −21.288 1.00 15.93 C ATOM 8857 C4 DMU 510 63.751 17.907 −20.014 1.00 130.14 C ATOM 8858 C40 DMU 510 52.472 24.084 −20.428 1.00 22.57 C ATOM 8859 C43 DMU 510 51.851 25.487 −20.508 1.00 23.10 C ATOM 8860 C5 DMU 510 67.395 14.647 −19.567 1.00 153.52 C ATOM 8861 C57 DMU 510 63.240 17.385 −18.650 1.00 106.97 C ATOM 8862 C6 DMU 510 61.877 17.425 −21.500 1.00 111.64 C ATOM 8863 C7 DMU 510 68.943 14.511 −19.570 1.00 149.84 C ATOM 8864 C8 DMU 510 69.702 15.843 −19.743 1.00 142.90 C ATOM 8865 C9 DMU 510 69.011 16.638 −20.867 1.00 138.50 C ATOM 8866 O1 DMU 510 67.683 17.019 −20.468 1.00 145.50 O ATOM 8867 O16 DMU 510 60.811 17.963 −22.257 1.00 93.04 O ATOM 8868 O2 DMU 510 69.551 16.577 −18.548 1.00 126.18 O ATOM 8869 O3 DMU 510 66.893 13.510 −20.227 1.00 153.38 O ATOM 8870 O4 DMU 510 69.335 13.597 −20.567 1.00 129.69 O ATOM 8871 O49 DMU 510 61.937 15.430 −22.901 1.00 103.89 O ATOM 8872 O5 DMU 510 62.653 18.436 −20.806 1.00 100.03 O ATOM 8873 O55 DMU 510 64.629 14.971 −22.282 1.00 126.79 O ATOM 8874 O6 DMU 510 69.294 18.527 −22.317 1.00 118.67 O ATOM 8875 O61 DMU 510 62.012 17.983 −18.323 1.00 77.40 O ATOM 8876 O7 DMU 510 65.525 16.240 −19.765 1.00 135.87 O ATOM 8877 C18 DMU 511 18.925 9.748 16.297 1.00 44.00 C ATOM 8878 C19 DMU 511 17.534 9.105 16.106 1.00 51.16 C ATOM 8879 C22 DMU 511 17.162 8.980 14.608 1.00 41.98 C ATOM 8880 C25 DMU 511 17.198 7.509 14.140 1.00 33.39 C ATOM 8881 C28 DMU 511 16.027 7.193 13.177 1.00 48.72 C ATOM 8882 C31 DMU 511 14.840 6.556 13.940 1.00 51.48 C ATOM 8883 C34 DMU 511 14.051 5.549 13.073 1.00 43.12 C ATOM 8884 C37 DMU 511 13.010 4.817 13.945 1.00 47.34 C ATOM 8885 C40 DMU 511 11.824 4.325 13.091 1.00 38.48 C ATOM 8886 C43 DMU 511 10.501 4.627 13.819 1.00 28.99 C ATOM 8887 O HOH 2 2.783 31.451 14.797 1.00 54.63 O ATOM 8888 O HOH 6 30.179 7.916 −24.831 1.00 41.19 O ATOM 8889 O HOH 7 7.986 38.338 14.733 1.00 32.37 O ATOM 8890 O HOH 8 42.716 −0.857 25.658 1.00 47.72 O ATOM 8891 O HOH 9 41.521 −3.114 28.145 1.00 59.36 O ATOM 8892 O HOH 10 11.506 19.784 15.060 1.00 13.55 O ATOM 8893 O HOH 11 7.044 26.934 11.072 1.00 20.10 O ATOM 8894 O HOH 12 −6.971 8.262 17.962 1.00 38.26 O ATOM 8895 O HOH 13 8.363 17.264 32.381 1.00 26.48 O ATOM 8896 O HOH 14 30.921 13.599 −15.216 1.00 20.42 O ATOM 8897 O HOH 15 29.552 9.877 −4.325 1.00 21.82 O ATOM 8898 O HOH 16 37.679 13.512 8.617 1.00 28.28 O ATOM 8899 O HOH 17 39.661 −0.205 5.263 1.00 60.94 O ATOM 8900 O HOH 18 17.910 −3.424 0.360 1.00 46.24 O ATOM 8901 O HOH 19 57.365 31.834 4.236 1.00 26.03 O ATOM 8902 O HOH 20 58.636 24.845 4.503 1.00 25.09 O ATOM 8903 O HOH 21 57.610 27.774 −6.483 1.00 31.23 O ATOM 8904 O HOH 22 62.365 30.490 −1.467 1.00 32.34 O ATOM 8905 O HOH 23 45.990 41.409 −11.157 1.00 39.81 O ATOM 8906 O HOH 24 36.124 0.372 −25.587 1.00 23.54 O ATOM 8907 O HOH 25 34.998 11.750 −21.896 1.00 28.39 O ATOM 8908 O HOH 26 22.086 5.561 −17.348 1.00 30.52 O ATOM 8909 O HOH 27 32.502 10.968 −29.158 1.00 41.93 O ATOM 8910 O HOH 28 39.530 18.364 −25.865 1.00 17.99 O ATOM 8911 O HOH 29 36.707 20.814 −43.464 1.00 21.15 O ATOM 8912 O HOH 30 43.882 15.460 −41.512 1.00 30.63 O ATOM 8913 O HOH 31 54.025 16.325 −43.651 1.00 43.31 O 

1. A method comprising: providing the coordinates of the turkey β1-AR structure listed in Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof.
 2. A method according to claim 1 further comprising predicting the three-dimensional structural representation of a target protein of unknown structure, or part thereof, by modelling the structural representation on all of the selected coordinates of the turkey β1-AR; and optionally aligning the amino acid sequence of the target protein of unknown structure with the amino acid sequence of turkey β1-AR listed in FIG. 7 to match homologous regions of the amino acid sequences prior to predicting the structural representation, and wherein modeling the structural representation comprises modeling the structural representation of the matched homologous regions of the target protein on the corresponding regions of the β1-AR to obtain a three dimensional structural representation for the target protein that substantially preserves the structural representation of the matched homologous regions.
 3. A method of claim 1 further comprising either (a) positioning the coordinates in the crystal unit cell of a target protein of unknown structure, or part thereof, so as to predict its structural representation, or (b) assigning NMR spectra peaks of the protein by manipulating the coordinates.
 4. A method of claim 1 further comprising providing an X-ray diffraction pattern of the target protein; and using the coordinates to predict at least part of the structure coordinates of the target protein. 5.-8. (canceled)
 9. A method of claim 1, further comprising using molecular modelling means to select or design one or more binding partners of β1-AR, wherein the three-dimensional structural representation of at least part of turkey β1-AR, as defined by the coordinates of turkey β1-AR listed in Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof, is compared with a three-dimensional structural representation of one or more candidate binding partners, and one or more binding partners that are predicted to interact with β1-AR are selected, optionally wherein the three-dimensional structural representation of the one or more candidate binding partners is obtained by: providing structural representations of a plurality of molecular fragments; fitting the structural representation of each of the molecular fragments to the coordinates of the turkey β1-AR listed in Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof; and assembling the representations of the molecular fragments into one or more representations of single molecules to provide the three-dimensional structural representation of one or more candidate binding partners.
 10. A method of claim 1 further comprising analyzing the interaction of one or more binding partners with β1-AR by a method comprising: providing a three dimensional structural representation of one or more binding partners to be fitted to the structural representation of β1-AR or selected coordinates thereof; and fitting the one of more binding partners to said structure. 11.-14. (canceled)
 15. A method according to claim 9, further comprising the steps of: obtaining or synthesising the one or more binding partners; and either: (I) contacting the one or more binding partners with a β1-AR to determine the ability of the one or more binding partners to interact with the β1-AR; or (II) forming one or more complexes of a β1-AR and a binding partner and analysing the one or more complexes by X-ray crystallography to determine the ability of the one or more binding partners to interact with β1-AR; or (III) forming one or more crystallised complexes of a β1-AR and a binding partner and analysing the one or more complexes by X-ray crystallography by employing the coordinates of the turkey β1-AR structure, listed in Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof, to determine the ability of the one or more binding partners to interact with the β1-AR, optionally wherein the one or more crystallised complexes are formed by either (a) providing a crystal of β1-AR and soaking the crystal with the binding partner to form a complex; or (b) mixing β1-AR with the binding partner and crystallising a β1-AR-binding partner complex. 16.-18. (canceled)
 19. A method for producing a binding partner of β1-AR comprising: identifying a binding partner according to the method of claim 9, and synthesising the binding partner.
 20. A binding partner produced by the method of claim 19, optionally wherein the binding partner is a full agonist, a partial agonist, an inverse agonist or an antagonist of β1-AR.
 21. A method of claim 1 further comprising: providing an X-ray diffraction pattern of β1-AR complexed with a β1-AR binding partner, or part thereof, which binds to β1-AR; and using said coordinates to predict at least part of the structure coordinates of the binding partner, optionally wherein the X-ray diffraction pattern is from a crystal formed either by (a) soaking a crystal of β1-AR with the binding partner to form a complex, or (b) mixing β1-AR with the binding partner and crystallising a β1-AR-binding partner complex, thereby predicting the three dimensional structure of a binding partner of unknown structure, or part thereof, which binds to β1-AR. 22.-26. (canceled)
 27. A pharmaceutical composition comprising the binding partner according to claim
 20. 28. A method of providing data for generating three dimensional structural representations of β1-AR, β1-AR homologues or analogues, complexes of β1-AR with binding partners, or complexes of β1-AR homologues or analogues with binding partners, or, for analysing or optimising binding of binding partners to said β1-AR or homologues or analogues, or complexes thereof, the method comprising: (i) establishing communication with a remote device containing computer-readable data comprising at least one of: (a) the coordinates of the turkey β1-AR structure provided in claim 1; (b) the coordinates of a target β1-AR homologue or analogue generated by homology modelling of the target based on the data in (a); (c) the coordinates of a binding partner generated by interpreting X-ray crystallographic data or NMR data by reference to the coordinates of the turkey β1-AR structure and (d) structure factor data derivable from the coordinates of (a), (b) or (c); and (ii) receiving said computer-readable data from said remote device.
 29. A method of claim 1 further comprising generating a three-dimensional structural representation of said coordinates, optionally wherein the three-dimensional structural representation is a computer generated representation or a physical representation, optionally wherein the computer used to generate the representation comprises: (i) a computer-readable data storage medium comprising a data storage material encoded with computer-readable data, wherein said data comprise the coordinates of the turkey β1-AR structure, listed in Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof; and (ii) instructions for processing the computer-readable data into a three-dimensional structural representation. 30.-32. (canceled)
 33. A method of claim 1 further comprising: analysing said coordinates to predict one or more sites of interaction; or analysing said coordinates to predict the location of internal and/or external parts of the structure; or performing a statistical and/or a topological analysis on the coordinates; and comparing the results of the analysis with the results of an analysis of coordinates of proteins of known activation states. 34.-37. (canceled)
 38. A computer system, intended to generate three dimensional structural representations of β1-AR, β1-AR homologues or analogues, complexes of β1-AR with binding partners, or complexes of β1-AR homologues or analogues with binding partners, or, to analyse or optimise binding of binding partners to said β1-AR or homologues or analogues, or complexes thereof, the system containing computer-readable data comprising one or more of: (a) the coordinates of the turkey β1-AR structure provided in claim 1; (b) the coordinates of a target β1-AR homologue or analogue generated by homology modelling of the target based on the data in (a); (c) the coordinates of a binding partner generated by interpreting X-ray crystallographic data or NMR data by reference to the coordinates of the turkey β1-AR structure, listed in Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof, and (d) structure factor data derivable from the coordinates of (a), (b) or (c).
 39. A computer system according to claim 38, comprising: (i) a computer-readable data storage medium comprising data storage material encoded with the computer-readable data; (ii) a working memory for storing instructions for processing the computer-readable data; and (iii) a central processing unit coupled to the working memory and to the computer-readable data storage medium for processing the computer-readable data to generate said structural representations or to analyse or optimise said binding; and optionally comprising a display coupled to the central-processing unit for displaying structural representations.
 40. (canceled)
 41. A computer-readable storage medium, comprising a data storage material encoded with (I) computer readable data, wherein the data comprises one or more of (a) the coordinates of the turkey β1-AR structure provided in claim 1; (b) the coordinates of a target β1-AR homologue or analogue generated by homology modelling of the target based on the data in (a); (c) the coordinates of a binding partner generated by interpreting X-ray crystallographic data or NMR data by reference to the coordinates of the turkey β1-AR structure, listed in Table A, Table B, Table C or Table D, optionally varied by a root mean square deviation of residue backbone atoms of not more than 1.235 Å, or selected coordinates thereof, and (d) structure factor data derivable from the coordinates of (a), (b) or (c); or (II) a first set of computer-readable data comprising a Fourier transform of at least a portion of the structural coordinates of turkey β1-AR provided in claim 1; which data, when combined with a second set of machine readable data comprising an X-ray diffraction pattern of a molecule or molecular complex of unknown structure, using a machine programmed with the instructions for using said first set of data and said second set of data, can determine at least a portion of the structure coordinates corresponding to the second set of machine readable data. 42.-44. (canceled)
 45. A method of producing a protein with a binding region that has substrate specificity substantially identical to that of β1-AR, the method comprising a) aligning the amino acid sequence of a target protein with the amino acid sequence of a β1-AR; b) identifying the amino acid residues in the target protein that correspond to any one or more of the following positions according to the numbering of the turkey β1-AR, as set out in (SEQ ID NO:4), 117, 118, 121, 122, 125, 201, 203, 207, 211, 215, 306, 307, 310 and 329; and c) making one or more mutations in the amino acid sequence of the target protein to replace one or more identified amino acid residues with the corresponding residue in the turkey β1-AR.
 46. A peptide of not more than 100 amino acid residues in length comprising at least five contiguous amino acid residues which define an external structural moiety of the β1-AR.
 47. (canceled)
 48. A mutant β1-AR, wherein the β1-AR before mutation has a binding region in the position equivalent to the binding region of turkey β1-AR that is defined by residues including 117, 118, 121, 122, 125, 201, 203, 207, 211, 215, 306, 307, 310 and 329 of β1-AR and wherein one or more residues equivalent to 117, 118, 121, 122, 125, 201, 203, 207, 211, 215, 306, 307, 310 and 329 forming part of the binding region of β1-AR is mutated.
 49. A method of making a β1-AR crystal comprising: providing purified β1-AR; and crystallising the β1-AR either by using the sitting drop or hanging drop vapour diffusion technique, using a precipitant solution comprising 0.1M ADA (N-(2-acetaimido) immunodiacetic acid) (pH5.6-9.5) and 25-35% PEG 600, optionally wherein the precipitant solution comprises 0.1M ADA (pH 6.9-7.3) and 29-32% PEG600.
 50. (canceled)
 51. A crystal of β1-AR having the structure defined by the coordinates of the β1-AR structure provided in claim
 1. 52.-56. (canceled) 